KR20220115489A - 헴, 코프로포르피린 ⅲ, 우로포르피린 ⅲ, 아연-코프로포르피린 ⅲ, 아연-우로포르피린 ⅲ 및 빌리버딘의 생산능력이 향상된 재조합 미생물, 및 이를 이용한 헴, 코프로포르피린 ⅲ, 우로포르피린 ⅲ, 아연-코프로포르피린 ⅲ, 아연-우로포르피린 ⅲ 및 빌리버딘의 생산방법 - Google Patents
헴, 코프로포르피린 ⅲ, 우로포르피린 ⅲ, 아연-코프로포르피린 ⅲ, 아연-우로포르피린 ⅲ 및 빌리버딘의 생산능력이 향상된 재조합 미생물, 및 이를 이용한 헴, 코프로포르피린 ⅲ, 우로포르피린 ⅲ, 아연-코프로포르피린 ⅲ, 아연-우로포르피린 ⅲ 및 빌리버딘의 생산방법 Download PDFInfo
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- KR20220115489A KR20220115489A KR1020210059751A KR20210059751A KR20220115489A KR 20220115489 A KR20220115489 A KR 20220115489A KR 1020210059751 A KR1020210059751 A KR 1020210059751A KR 20210059751 A KR20210059751 A KR 20210059751A KR 20220115489 A KR20220115489 A KR 20220115489A
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- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
본 발명은 헴 (heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ), 우로포르피린 Ⅲ (uroporphyrin Ⅲ), 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ), 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ) 및 빌리버딘 (Biliverdin)의 생산능력이 향상된 재조합 미생물, 이의 제조방법 및 이를 이용한 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘의 생산방법에 관한 것이다. 본 발명에서는 재조합 미생물의 포르피린 생산능 향상 효과를 통해 5-아미노레불린산 (5-aminolevulinic acid, ALA)의 합성을 위한 C4 및 C5 경로 관련 유전자의 도입, 코프로포르피린 Ⅲ 의존성 경로 관련 유전자의 도입 및 전사조절인자의 도입을 통한 시너지 효과를 처음 입증하였으며, 또한 종래 재조합 미생물에서 외분비 단백질을 도입하여 세포외 생산을 유도한 것과 달리 최초로 상기 미생물의 세포벽을 개량하는 전략을 통해 헴의 세포외 분비를 현저히 증가시킬 수 있음을 확인하였다. 이에, 본 발명에 따른 재조합 미생물은 상기와 같은 대사공학적 전략을 통해 포르피린 계열 물질의 생산능력이 강화되어 높은 생산능을 나타내는바, 본 발명의 재조합 미생물을 이용하면 고부가가치의 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘을 경제적이고 효율적으로 생산할 수 있다.
Description
본 발명은 헴 (heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ), 우로포르피린 Ⅲ (uroporphyrin Ⅲ), 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ), 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ) 및 빌리버딘 (Biliverdin)의 생산능력이 향상된 재조합 미생물, 이의 제조방법 및 이를 이용한 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘의 생산방법에 관한 것이다.
헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘과 같은 포르피린 (porphyrin)은 네 개의 피롤 (pyrrole)이 메틴 (methine) 그룹으로 연결된 이종고리식 거대유기화합물 (heterocyclic macrocyle organic compound)이다. 헴 및 포르피린 유사체들은 숙시닐-코에이 (succinyl-CoA)와 글리신 (glycine)의 중합반응에 의한 경로 (C4 경로) 또는 글루타메이트 (glutamate)를 출발물질로 하여 ATP, NADPH 조효소를 사용하는 경로 (C5 경로)를 통하여 생체 내에서 합성된다. 이 두 경로에 대한 선호도는 종에 따라 다르며, 구체적으로 C4 경로의 경우 5-아미노레불린산 합성효소 (5-aminolevulinic acid synthase, ALAS)의 작용, C5 경로의 경우 글루타메이트로부터 글루타밀-tRNA 합성효소 (glutamyl-tRNA synthetase; GltX), 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA) 및 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL)의 작용에 의한 5-아미노레불린산 (5-aminolevulinic acid, ALA)의 합성으로부터 헴 대사경로가 시작된다. 2분자의 5-아미노레불린산은 포르포빌리노겐 합성효소 (porphobilinogen synthase, HemB)가 촉매하는 축합 (condensation) 반응을 통해 포르포빌리노겐 (porphobilinogen, PBG)으로 합성되고, 4분자의 포르포빌리노겐은 포르포빌리노겐 디아미네이즈 (porphobilinogen deaminase, HemC)의 촉매 작용을 통해 1-하이드록시메틸빌란 (1-hydroxymethylbilane, HMB)으로 합성된다. 1-하이드록시메틸빌란은 우로포르피리노겐 Ⅲ 합성효소 (uroporphyrinogen Ⅲ synthase, HemD)에 의해 고리화되어 포르피린의 기본 골격인 우로포르피리노겐 Ⅲ (uroporphyrinogen Ⅲ)로 합성된다.
이후 우로포르피리노겐 Ⅲ로부터 헴이 합성되는 방식은 종에 따라 세 가지 경로를 통해 진행된다. 첫 번째는 네 가지 효소 반응으로 구성된 프로토포르피린 IX 의존성 경로 (protoporphyrin IX-dependent pathway)로 생물학 및 생화학 분야에서 잘 알려져 있으며 주로 프로테오박테리아 (Proteobacteria) 및 진핵생물에서 발견된다. 두 번째는 황산염 환원 세균 (sulfate reducing bacteria)와 고세균 (archaea)에서 발견되는 원시 헴 경로로, 6가지 효소 반응을 통해 헴을 합성한다. 마지막은 네 가지 효소 반응으로 구성된 코프로포르피린 Ⅲ 의존성 경로 (coproporphyrin Ⅲ-dependent pathway)로, 최근에 발견된 방선균 (actinobacteria)과 후벽균 (firmicutes)에서 발견된다. 코프로포르피린 Ⅲ 의존성 경로와 프로토포르피린 IX 의존성 경로에서 우로포르피리노겐 Ⅲ를 코프로피리노겐 Ⅲ (coproporphyrinogen Ⅲ, CPG Ⅲ)로 전환시키는 반응은 우로포르피리노겐 Ⅲ 디카복실레이즈 (uroporphyrinogen Ⅲ decarboxylase, HemE)에 의해 진행된다. 코프로포르피린 Ⅲ 의존성 경로에서는 코프로포르피리노겐 Ⅲ (coproporhyrinogen Ⅲ)가 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY)에 의해 코프로포르피린 Ⅲ (coproporhyrin Ⅲ)로 전환된다. 이어서 코프로포르피린 Ⅲ로부터 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH)에 의해 철이온 첨가로 코프로-헴 (copro-heme)이 합성되고, 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ)에 의해 코프로-헴은 최종적으로 헴으로 전환된다. 빌리버딘은 헴 옥시게네이즈 (Heme oxygenase, HmuO)에 의해 헴이 분해되어 형성된다.
헴은 호흡, 산소 전달, 광합성, 전자전달과 관련된 생명체의 필수 보조인자로 식품 산업에서 유기 철 보충제뿐만 아니라 의료 분야의 급성 간헐성 포르피린증 (acute intermittent porphyria)에 대한 생체 이용 및 제약 화합물로 널리 사용되고 있다. 또한 헴은 최근 식품 산업에서 인공육의 주요 원료로 활발히 사용되고 있다.
아연 포르피린 유도체는 최근 빛을 수확하여 태양 에너지를 전기 에너지로 변환하는 태양전지의 광감응제로 이용되거나 인터페이스 (interface)에서 다단계 반응을 촉매하는 촉매제로 주목받고 있다. 전자 및 물리 화학적 응용 외에도 아연 포르피린은 항종양 및 항균활성에 대한 광감응제로 광역학치료 (photodynamic therapy)에서 이용되고 있다.
빌리버딘은 항산화 성질을 가져 유용한 생리적 기능을 수행할 수 있으며, 퍼옥시라디칼의 강력한 제거제로 알려져 있다. 빌리버딘은 돌연변이 유발 물질인 다환 방향족 탄화수소, 헤테로사이클릭아민 및 산화제의 영향을 억제하는 효과가 있는 것으로 확인되었으며, 일부 연구에 따르면 체내에 빌리버딘의 농도가 높은 사람들은 암 및 심혈관 질환의 빈도가 낮다고 보고된바 있다.
종래 헴 생합성을 향상시키기 위한 연구로는 대장균을 통해 수행된 바 있으며 C5 경로, 프로토포르피린 IX 의존성 경로를 포함하는 헴 생합성 경로 강화를 통해 헴 생산을 증대시킨 결과가 보고되어 있다. 또한 헴 및 다른 포르피린 계열 물질의 생산을 증대시키기 위한 재조합 균주 및 이의 생산 효과가 일부 보고되고 있으나, 포르피린 및 이의 유사체를 보다 효율적으로 고생산하고 세포외 분비능을 더욱 증대시킨 재조합 미생물 및 최적화된 방법에 대한 연구개발이 추가적으로 필요한 실정이다.
이에, 본 발명자들은 L-글루탐산 (L-glutamic acid) 생성능을 갖는 미생물을 이용하여 헴을 포함한 다양한 포르피린의 생산능이 향상된 재조합 미생물을 개발하고자 연구 노력한 결과, 헴의 전구물질인 5-아미노레불린산을 과생산하는 C4 및 C5 경로 유전자, 코프로포르피린 Ⅲ 의존성 경로 관련 유전자 및 전사조절인자의 도입, 해당 미생물의 세포벽 개량 전략을 적용함으로써 헴을 비롯한 포르피린 및 이의 유사체의 생산능력 및 이의 외분비가 향상된 재조합 미생물을 제조하였는바, 이에 기초하여 본 발명을 완성하였다.
이에, 본 발명은 헴 (Heme), 코프로포르피린 Ⅲ (Coproporphyrin Ⅲ) 및 우로포르피린 Ⅲ (Uroporphyrin Ⅲ) 생산능력이 향상된 재조합 미생물을 제공하는 것을 목적으로 한다.
또한, 본 발명은 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ) 생산능력이 향상된 재조합 미생물을 제공하는 것을 다른 목적으로 한다.
또한, 본 발명은 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물을 제공하는 것을 또 다른 목적으로 한다.
또한, 본 발명은 상기 재조합 미생물의 제조방법을 제공하는 것을 또 다른 목적으로 한다.
또한, 본 발명은 상기 재조합 미생물을 배양하는 단계를 포함하는, 헴의 생산방법을 제공하는 것을 또 다른 목적으로 한다.
또한, 본 발명은 상기 재조합 미생물을 배양하는 단계를 포함하는, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산방법을 제공하는 것을 또 다른 목적으로 한다.
또한, 본 발명은 상기 재조합 미생물을 배양하는 단계를 포함하는, 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ의 생산방법을 제공하는 것을 또 다른 목적으로 한다.
또한, 본 발명은 상기 재조합 미생물을 배양하는 단계를 포함하는, 빌리버딘의 생산방법을 제공하는 것을 또 다른 목적으로 한다.
그러나 본 발명이 이루고자 하는 기술적 과제는 이상에서 언급한 과제에 제한되지 않으며, 언급되지 않은 또 다른 과제들은 아래의 기재로부터 당업자에게 명확하게 이해될 수 있을 것이다.
상기와 같은 본 발명의 목적을 달성하기 위하여, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자가 도입된, 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물을 제공한다.
본 발명의 일구현예로, 상기 재조합 미생물은 추가적으로 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된 것일 수 있다.
본 발명의 다른 구현예로, 상기 재조합 미생물은 HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되고; 및 HrrS, HtaA 및 HmuT를 암호화하는 유전자의 발현이 억제된 것일 수 있다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자가 도입된, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물을 제공한다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈 (Heme oxygenase, HmuO)를 암호화하는 유전자가 도입된, 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물을 제공한다.
또한, 본 발명은 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된, 헴 (Heme)의 외분비능이 향상된 재조합 미생물을 제공한다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
본 발명의 일구현예로, 상기 제조방법은 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현을 억제시키는 단계를 추가로 포함할 수 있다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
또한, 본 발명은 글루탐산(glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈(Heme oxygenase, HmuO)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
본 발명의 일구현예로, 상기 글루탐산 생성능을 가지는 미생물은 코리네박테리움 글루타믹쿰 (Corynebacterium glutamicum)일 수 있다.
본 발명의 다른 구현예로, 상기 HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ, HrtA, HrtAB 및 HmuO는 각각 서열번호 1 내지 11로 표시되는 아미노산 서열로 이루어진 것일 수 있다.
본 발명의 또 다른 구현예로, 상기 HrrS, HtaA 및 HmuT은 각각 서열번호 13 내지 15로 표시되는 아미노산 서열로 이루어진 것일 수 있다.
또한, 본 발명은 하기 단계를 포함하는, 헴 (Heme)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 철 이온 (Fe2+)을 포함하는 배지에서 배양하여 헴을 생성시키는 단계; 및
(b) 상기 생성된 헴을 추출 및 수득하는 단계.
본 발명의 일구현예로, 상기 단계 (a)에서 배지 내에 5 내지 100mg/L 농도의 에탐부톨 (ethambutol)이 추가로 포함될 수 있다.
본 발명의 다른 구현예로, 상기 단계 (a)에서 배지는 질소원으로 트립톤 (Tryptone)이 포함된 것일 수 있다.
본 발명의 또 다른 구현예로, 상기 배양은 유가식 발효 공정으로 이루어지는 것일 수 있다.
또한, 본 발명은 하기 단계를 포함하는, 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 배지에서 배양하여 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 추출 및 수득하는 단계.
또한, 본 발명은 하기 단계를 포함하는, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 아연 이온 (Zn2+)을 포함하는 배지에서 배양하여 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 추출 및 수득하는 단계.
또한, 본 발명은 하기 단계를 포함하는, 빌리버딘 (Biliverdin)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 배지에서 배양하여 빌리버딘을 생성시키는 단계; 및
(b) 상기 생성된 빌리버딘을 추출 및 수득하는 단계.
본 발명에서는 재조합 미생물의 포르피린 생산능 향상 효과를 통해 5-아미노레불린산 (5-aminolevulinic acid, ALA)의 합성을 위한 C4 및 C5 경로 관련 유전자의 도입, 코프로포르피린 Ⅲ 의존성 경로 관련 유전자의 도입 및 전사조절인자의 도입을 통한 시너지 효과를 처음 입증하였으며, 또한 종래 재조합 미생물에서 외분비 단백질을 도입하여 세포외 생산을 유도한 것과 달리 최초로 상기 미생물의 세포벽을 개량하는 전략을 통해 헴의 세포외 분비를 현저히 증가시킬 수 있음을 확인하였다. 이에, 본 발명에 따른 재조합 미생물은 상기와 같은 대사공학적 전략을 통해 포르피린 계열 물질의 생산능력이 강화되어 높은 생산능을 나타내는바, 본 발명의 재조합 미생물을 이용하면 고부가가치의 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘을 경제적이고 효율적으로 생산할 수 있다.
도 1은 각각 야생형 코리네박테리움 글루타믹쿰 (WT), S, AL 및 ALS 재조합 균주를 플라스크 배양한 후 세포 성장 (Cell growth), 글루코오스 (Glucose), 글루타메이트 (Glutamate) 및 글리신 (Glycine) 소비량과 함께 헴 (Heme), 5-아미노레불린산 (ALA), 코프로포르피린 Ⅲ (CP Ⅲ), 우로포르피린 Ⅲ (UP Ⅲ)의 생산량을 측정한 결과이다.
도 2는 hemY, hemH, hemQ 및/또는 dtxR 유전자가 도입된 재조합 균주를 플라스크 배양한 후 헴 생산 및 mRNA 발현수준을 측정한 결과를 나타낸 것으로, 도 2a는 ALS, ALS-Y, ALS-H, ALS-Q, ALS-HQ 및 ALS-YHQ 재조합 균주에서 각각 헴, 코프로포르피린 Ⅲ (CP Ⅲ), 우로포르피린 Ⅲ (UP Ⅲ)의 생산량을 측정한 결과이고, 도 2b는 ALSdt, ALSdt-Y, ALSdt-H, ALSdt-Q, ALSdt-HQ, ALSdt-YHQ 재조합 균주에서 각각 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ의 생산량을 측정한 결과이며, 도 2c는 각각 ALS-H 및 ALSdt-H에서 mRNA 발현수준을 측정한 결과이다.
도 3은 세포벽 개량 전략이 적용된 재조합 균주에서 헴 생산을 측정한 결과로서, 도 3a는 본 발명에 따른 코리네박테리움 글루타믹쿰 균주의 세포벽 개량 전략을 그림으로 도시한 것이고, 도 3b는 ALSdt-YHQ, ALSdt-YHQBA, ALSdt-YHQcA, ΔS::ALSdt-YHQBA, ΔSA::ALSdt-YHQBA, ΔSAT::ALSdt-YHQBA, ΔSAT::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 각각 세포 성장과 함께 총 헴 (Total heme), 외분비 헴 (Secreted heme), 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ 생산 수준을 측정한 결과이다.
도 4는 ALSdt-YHQ, ALSdt-YHQBA, ALSdt-YHQcA, ΔS::ALSdt-YHQBA, ΔSA::ALSdt-YHQBA, ΔSAT::ALSdt-YHQBA, ΔSAT::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 총 우로포르피린 Ⅲ (Total UP Ⅲ) 및 외분비된 우로포르피린 Ⅲ (Secreted UP Ⅲ) 수준을 각각 측정한 결과이다.
도 5는 질소원을 최적화하기 위하여 ΔSAT::ALSdtE-YHQBA 재조합 균주를 상이한 질소원이 포함된 각 mCGXII-Y10 배지 (mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca)에서 플라스크 배양한 후 세포 성장과 함께 세포 내외의 헴 생산 수준을 측정한 결과이다.
도 6은 ΔSAT::ALSdtE-YHQBA2 균주를 각각 mCGXII 배지, mCGXII에 에탐부톨이 첨가된 배지 (mCGXII + ETB) 및 mCGXII-Tr 배지에서 유가식 발효공정으로 배양하면서 세포 성장 및 글루코오스 소비와 함께 세포 내외의 헴 생산 수준을 측정한 결과이다.
도 7은 ΔSAT::ALSdtE-YHQBA와 ΔSATO::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 세포 내외의 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ 생산 수준을 측정한 결과이다.
8은 ALSdtE, ΔLdh::ALSdtE, ALSdtE-BA 재조합 균주를 플라스크 배양한 후 세포 성장과 함께 각각 세포 내외의 총 아연-포르피린 (ZnPP), 아연-코프로포르피린 Ⅲ (Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-UP Ⅲ)의 생산 수준을 측정한 결과이다.
도 9는 에탐부톨 농도를 최적화하기 위하여 ALSdtE 균주를 에탐부톨이 다양한 농도 (5, 25, 50, 100mg/L)로 첨가된 조건에서 플라스크 배양한 후 세포 성장과 함께 세포 내외의 아연-포르피린, 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ의 생산 수준을 측정한 결과이다.
도 10은 ALSdtE 균주를 유가식 발효공정으로 배양하면서 세포 성장 및 글루코오스 소비와 함께 세포 내외의 아연-포르피린 (Zn-porphyrin) 수준을 측정한 결과이다.
도 11은 ALSdtE-YHQ 및 ALSdtE-YHQO 재조합 균주를 CGXII 배지에서 프라스크 배양한 후 헴, 코프로포르피린 Ⅲ 및 빌리버딘 (Biliverdin)의 생산 수준을 각각 측정한 결과이다.
도 12는 본 발명에 따른 재조합 미생물에 대한 대사공학 전략을 종합하여 모식도로 나타낸 것이다.
도 2는 hemY, hemH, hemQ 및/또는 dtxR 유전자가 도입된 재조합 균주를 플라스크 배양한 후 헴 생산 및 mRNA 발현수준을 측정한 결과를 나타낸 것으로, 도 2a는 ALS, ALS-Y, ALS-H, ALS-Q, ALS-HQ 및 ALS-YHQ 재조합 균주에서 각각 헴, 코프로포르피린 Ⅲ (CP Ⅲ), 우로포르피린 Ⅲ (UP Ⅲ)의 생산량을 측정한 결과이고, 도 2b는 ALSdt, ALSdt-Y, ALSdt-H, ALSdt-Q, ALSdt-HQ, ALSdt-YHQ 재조합 균주에서 각각 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ의 생산량을 측정한 결과이며, 도 2c는 각각 ALS-H 및 ALSdt-H에서 mRNA 발현수준을 측정한 결과이다.
도 3은 세포벽 개량 전략이 적용된 재조합 균주에서 헴 생산을 측정한 결과로서, 도 3a는 본 발명에 따른 코리네박테리움 글루타믹쿰 균주의 세포벽 개량 전략을 그림으로 도시한 것이고, 도 3b는 ALSdt-YHQ, ALSdt-YHQBA, ALSdt-YHQcA, ΔS::ALSdt-YHQBA, ΔSA::ALSdt-YHQBA, ΔSAT::ALSdt-YHQBA, ΔSAT::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 각각 세포 성장과 함께 총 헴 (Total heme), 외분비 헴 (Secreted heme), 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ 생산 수준을 측정한 결과이다.
도 4는 ALSdt-YHQ, ALSdt-YHQBA, ALSdt-YHQcA, ΔS::ALSdt-YHQBA, ΔSA::ALSdt-YHQBA, ΔSAT::ALSdt-YHQBA, ΔSAT::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 총 우로포르피린 Ⅲ (Total UP Ⅲ) 및 외분비된 우로포르피린 Ⅲ (Secreted UP Ⅲ) 수준을 각각 측정한 결과이다.
도 5는 질소원을 최적화하기 위하여 ΔSAT::ALSdtE-YHQBA 재조합 균주를 상이한 질소원이 포함된 각 mCGXII-Y10 배지 (mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca)에서 플라스크 배양한 후 세포 성장과 함께 세포 내외의 헴 생산 수준을 측정한 결과이다.
도 6은 ΔSAT::ALSdtE-YHQBA2 균주를 각각 mCGXII 배지, mCGXII에 에탐부톨이 첨가된 배지 (mCGXII + ETB) 및 mCGXII-Tr 배지에서 유가식 발효공정으로 배양하면서 세포 성장 및 글루코오스 소비와 함께 세포 내외의 헴 생산 수준을 측정한 결과이다.
도 7은 ΔSAT::ALSdtE-YHQBA와 ΔSATO::ALSdtE-YHQBA 재조합 균주를 에탐부톨 (ETB)의 첨가 또는 미첨가 조건에서 플라스크 배양한 후 세포 내외의 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ 생산 수준을 측정한 결과이다.
8은 ALSdtE, ΔLdh::ALSdtE, ALSdtE-BA 재조합 균주를 플라스크 배양한 후 세포 성장과 함께 각각 세포 내외의 총 아연-포르피린 (ZnPP), 아연-코프로포르피린 Ⅲ (Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-UP Ⅲ)의 생산 수준을 측정한 결과이다.
도 9는 에탐부톨 농도를 최적화하기 위하여 ALSdtE 균주를 에탐부톨이 다양한 농도 (5, 25, 50, 100mg/L)로 첨가된 조건에서 플라스크 배양한 후 세포 성장과 함께 세포 내외의 아연-포르피린, 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ의 생산 수준을 측정한 결과이다.
도 10은 ALSdtE 균주를 유가식 발효공정으로 배양하면서 세포 성장 및 글루코오스 소비와 함께 세포 내외의 아연-포르피린 (Zn-porphyrin) 수준을 측정한 결과이다.
도 11은 ALSdtE-YHQ 및 ALSdtE-YHQO 재조합 균주를 CGXII 배지에서 프라스크 배양한 후 헴, 코프로포르피린 Ⅲ 및 빌리버딘 (Biliverdin)의 생산 수준을 각각 측정한 결과이다.
도 12는 본 발명에 따른 재조합 미생물에 대한 대사공학 전략을 종합하여 모식도로 나타낸 것이다.
본 발명자들은 L-글루탐산 (L-glutamic acid) 생성능을 갖는 미생물에 헴의 전구물질인 5-아미노레불린산을 과생산하는 C4 및 C5 경로 유전자, 코프로포르피린 Ⅲ 의존성 경로 관련 유전자 및 전사조절인자의 도입, 해당 미생물의 세포벽 개량 전략을 적용함으로써 헴 및 다양한 포르피린의 생산능력 및 이의 외분비 능력이 향상된 재조합 미생물을 제조하였다.
이에, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자가 도입된, 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물을 제공한다.
본 발명에 있어서, 상기 재조합 미생물은 추가적으로 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된 것일 수 있다.
본 발명에 있어서, 상기 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산능력이 향상된 재조합 미생물은 하기 재조합 미생물을 모두 포함한다.
i) HemA, HemL 및 AlaS를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅱ) HemA, HemL, AlaS 및 DtxR를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅲ) HemA, HemL, AlaS, DtxR 및 HemE를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅳ) HemA, HemL, AlaS, DtxR 및 HemY를 암호화하는 유전자가 도입된, 재조합 미생물;
v) HemA, HemL, AlaS, DtxR 및 HemH를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅵ) HemA, HemL, AlaS, DtxR 및 HemQ를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅶ) HemA, HemL, AlaS, DtxR, HemH 및 HemQ를 암호화하는 유전자가 도입된, 재조합 미생물;
ⅷ) HemA, HemL, AlaS, DtxR, HemY, HemH 및 HemQ를 암호화하는 유전자가 도입된, 재조합 미생물; 및
ⅸ) HemA, HemL, AlaS, DtxR, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입된, 재조합 미생물.
또한, 본 발명은 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된, 헴 (Heme)의 외분비능이 향상된 재조합 미생물을 제공한다.
본 발명에 있어서, 하기의 재조합 미생물은 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산능력이 향상되고, 세포벽의 헴 결합능이 감소되어 헴 외분비능이 향상된 것일 수 있다.
i) HemA, HemL, AlaS, DtxR, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되어 있고, HrrS를 암호화하는 유전자의 발현이 억제된, 재조합 미생물;
ⅱ) HemA, HemL, AlaS, DtxR, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되어 있고, HrrS 및 HtaA를 암호화하는 유전자의 발현이 억제된, 재조합 미생물;
ⅲ) HemA, HemL, AlaS, DtxR, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되어 있고, HrrS, HtaA 및 HmuT를 암호화하는 유전자의 발현이 억제된, 재조합 미생물; 및
ⅳ) HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되어 있고, HrrS, HtaA 및 HmuT를 암호화하는 유전자의 발현이 억제된, 재조합 미생물.
본 발명에 있어서, 바람직하게 상기 재조합 미생물은 HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되고; 및 HrrS, HtaA 및 HmuT를 암호화하는 유전자의 발현이 억제된 것일 수 있다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자가 도입된, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물을 제공한다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈(Heme oxygenase, HmuO)를 암호화하는 유전자가 도입된, 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물을 제공한다.
본 발명에서, 상기 HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ, HrtA, HrtB 및 HmuO는 각각 서열번호 1 내지 11로 표시되는 아미노산 서열로 이루어진 것일 수 있다. 또한 상기 HrrS, HtaA 및 HmuT은 각각 서열번호 13 내지 15로 표시되는 아미노산 서열로 이루어진 것일 수 있다. 이때, 상기 각 단백질들은 서열번호 1 내지 11, 13 내지 15로 표시되는 아미노산 서열과 70% 이상, 바람직하게는 80% 이상, 더욱 바람직하게는 90% 이상, 가장 바람직하게는 95%, 96%, 97%, 98%, 99% 이상의 서열 상동성을 가지는 아미노산 서열을 포함할 수 있다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
본 발명에서, 상기 제조방법은 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현을 억제시키는 단계를 추가로 포함할 수 있다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
또한, 본 발명은 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈(Heme oxygenase, HmuO)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 상기 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물의 제조방법을 제공한다.
본 발명에서 사용되는 용어, “재조합 미생물”은 유전자재조합 기술로 도입된 유전자재조합 DNA에 의하여 유전물질이 재조합된 미생물을 말한다. 상기 유전자재조합 DNA는 어떤 세포 내에서 복제 가능한 DNA (운반체)와 이종의 DNA를 효소 등을 이용하여 시험관 안에서 결합시켜 제작한 DNA를 말한다.
본 발명에 있어서, 바람직하게 재조합 미생물은 글루탐산 생성능을 가지는 미생물을 유전자재조합 기술을 통해 포르피린 계열 물질, 바람직하게 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및/또는 빌리버딘의 생산능이 향상된 것일 수 있고, 상기 글루탐산 생성능을 가지는 미생물은 바람직하게 코리네박테리움 글루타믹쿰 (Corynebacterium glutamicum)일 수 있다.
본 발명에서 사용되는 용어, “벡터 (vector)”는 적합한 숙주 내에서 DNA를 발현시킬 수 있는 적합한 조절 서열에 작동가능하게 연결된 DNA 서열을 함유하는 DNA 제조물을 의미한다. 벡터는 플라스미드, 파지 입자 또는 간단하게 잠재적 게놈 삽입물일 수 있다. 적당한 숙주로 형질전환되면, 벡터는 숙주 게놈과 무관하게 복제하고 기능할 수 있거나, 또는 일부 경우에 게놈 그 자체에 통합될 수 있다. 플라스미드가 현재 벡터의 가장 통상적으로 사용되는 형태이므로, 본 발명의 명세서에서 “플라스미드 (plasmid)” 및 “벡터 (vector)”는 때로 상호 교환적으로 사용된다.
본 발명의 목적상, 플라스미드 벡터를 이용하는 게 바람직하다. 이러한 목적에 사용될 수 있는 전형적인 플라스미드 벡터는 (a) 숙주세포당 수 개에서 수백 개의 플라스미드 벡터를 포함하도록 복제가 효율적으로 이루어지도록 하는 복제 개시점, (b) 플라스미드 벡터로 형질전환된 숙주세포가 선발될 수 있도록 하는 항생제 내성 유전자 및 (c) 외래 DNA 절편이 삽입될 수 있는 제한효소 절단부위를 포함하는 구조를 지니고 있다. 적절한 제한효소 절단부위가 존재하지 않을지라도, 통상의 방법에 따른 합성 올리고뉴클레오타이드 어댑터 (oligonucleotide adaptor) 또는 링커 (linker)를 사용하면 벡터와 외래 DNA를 용이하게 라이게이션 (ligation)할 수 있다.
본 발명에서 용어 “재조합 벡터”는 통상 이종의 DNA의 단편이 삽입된 재조합 캐리어 (recombinant carrier)로서 일반적으로 이중 가닥의 DNA의 단편을 의미한다. 여기서, 이종 DNA는 숙주 세포에서 천연적으로 발견되지 않는 DNA인 이형 DNA를 의미한다. 재조합 벡터는 일단 숙주 세포 내에 있으면 숙주 염색체 DNA와 무관하게 복제할 수 있으며 벡터의 수 개의 카피 및 그의 삽입된 (이종) DNA가 생성될 수 있다. 이후 상기 재조합 벡터는 숙주세포에 형질전환 또는 트랜스펙션 (transfection) 될 수 있다.
본 발명에 사용된 용어 “형질전환”은 DNA를 숙주로 도입하여 DNA가 염색체 외 인자로서 또는 염색체 통합완성에 의해 복제 가능하게되는 것을 의미한다. 물론 모든 벡터가 본 발명의 DNA 서열을 발현하는데 모두 동등하게 기능을 발휘하지는 않는다는 것을 이해하여야만 한다. 마찬가지로 모든 숙주가 동일한 발현 시스템에 대해 동일하게 기능을 발휘하지는 않는다. 그러나, 당업자라면 과도한 실험적인 부담 없이 본 발명의 범위를 벗어나지 않는 채로 여러 벡터, 발현 조절 서열 및 숙주 중에서 적절한 선택을 할 수 있다. 예를 들어, 벡터를 선택함에 있어서는 숙주를 고려하여야 하는데, 이는 벡터가 그 안에서 복제되어야만 하기 때문이다. 벡터의 복제 수, 복제 수를 조절할 수 있는 능력 및 당해 벡터에 의해 코딩되는 다른 단백질, 예를 들어 항생제 마커의 발현도 또한 고려되어야만 한다.
상기 “형질전환” 또는 “트랜스펙션”은 원핵 또는 진핵 숙주세포 내로 외인성 핵산 (DNA 또는 RNA)을 도입하는 데에 통상 사용되는 여러 종류의 다양한 기술, 예컨대 전기천공법 (electroporation), 인산칼슘 침전법, DEAE-덱스트란 트랜스펙션 또는 리포펙션 (lipofection) 등을 사용할 수 있으나, 이에 제한되는 것은 아니며 당업자가 적절히 선택하여 이용할 수 있다.
당업계에 주지된 바와 같이, 숙주세포에서 형질전환 유전자의 발현 수준을 높이기 위해서는, 해당 유전자가 선택된 발현 숙주 내에서 기능을 발휘하는 전사 및 해독 발현 조절 서열에 작동가능하도록 연결되어야만 한다. 바람직하게는 발현 조절서열 및 해당 유전자는 세균 선택 마커 및 복제 개시점 (replication origin)을 같이 포함하고 있는 하나의 재조합 벡터 내에 포함되게 된다. 숙주세포가 진핵세포인 경우에는, 재조합벡터는 진핵 발현 숙주 내에서 유용한 발현 마커를 더 포함하여야만 한다.
본 발명에 있어서, 선호되는 숙주세포는 원핵세포일 수 있고, 바람직하게 상기 원핵 숙주세포는 C. glutamicum ATCC 13826, C. glutamicum ATCC 13032, C. glutamicum 13059, C. glutamicum ATCC 14067, C. glutamicum ATCC 13761, C. glutamicum ATCC 13058, C. glutamicum ATCC 13745 등을 포함할 수 있으나, 이에 제한되는 것은 아니다. 또한, E.coli DH5α, E.coli JM101, E.coli TOP10, E.coli K12, E.coli W3110, E.coli X1776, E.coli XL1-Blue (Stratagene), E.coli B, E.coli BL21 등과 같은 E.coli 균주 및 다른 원핵생물의 종 (species) 및 속 (genera)에 포함되는 균주가 사용될 수 있다.
본 발명에서, 숙주세포에서 상기 유전자의 발현 억제는 CRISPR 기술을 이용하여 표적 유전자의 발현을 억제함으로써 이루어질 수 있으며, 바람직하게는 CRISPR용 재조합 벡터를 이용할 수 있고, 더욱 바람직하게는 pJYS1_Peftu 및 pJYS2_crtYf의 공지된 벡터를 이용할 수 있으나, 유전자의 발현 억제 방법이 이것으로 제한되는 것은 아니며 당업자가 공지된 기술을 적절히 선택하여 이용할 수 있다.
본 발명의 구체적인 실시예에서는, 본 발명에 따른 다양한 재조합 균주를 배양한 후 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 또는 빌리버딘 (Biliverdin) 각각을 추출함으로써 생산량을 측정 및 비교하였고, 상기 각 물질의 가장 높은 생산량을 달성하기 위한 배양 조건, 예컨대 배지 내 질소원, 배양방법 및 에탐부톨의 농도를 최적화하였다.
이에, 본 발명의 다른 양태로서, 본 발명은 하기 단계를 포함하는, 헴 (Heme)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 철 이온 (Fe2+)을 포함하는 배지에서 배양하여 헴을 생성시키는 단계; 및
(b) 상기 생성된 헴을 추출 및 수득하는 단계.
또한, 본 발명은 하기 단계를 포함하는, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 아연 이온 (Zn2+)을 포함하는 배지에서 배양하여 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 추출 및 수득하는 단계.
본 발명에 있어서, 상기 각 (a) 단계에서 배지는 바람직하게 CGXII 배지에 효모 추출물이 첨가된 mCGXII-Y10 배지일 수 있고, 더욱 바람직하게는 상기 mCGXII-Y10 배지에 질소원으로 (NH4)2SO4, NH4Cl, 트립톤 및 카제인가수분해물이 각각 첨가된 mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca 배지일 수 있으며, 가장 바람직하게는 트립톤이 첨가된 mCGXII-Tr일 수 있다.
본 발명에 있어서, 상기 각 (a) 단계에서 배지는 에탐부톨 (ethambutol)이 추가로 첨가된 것일 수 있으며, 에탐부톨은 바람직하게 5 내지 100mg/L, 더욱 바람직하게 5 내지 50mg/L, 더더욱 바람직하게는 10 내지 25mg/L, 가장 바람직하게는 25mg/L의 농도로 포함될 수 있다.
본 발명에 있어서, 상기 배양은 재조합 미생물, 바람직하게 재조합 코리네박테리움 글루타믹쿰의 성장이 가능한 조건에서 특별한 제한 없이 이루어질 수 있으며, 바람직하게는 유가식 발효 공정으로 수행될 수 있으나, 이에 제한되는 것은 아니다.
본 발명에서 사용되는 용어, “유가식 발효”란 미생물의 배양방법 중 액체배양의 한 종류로서 기질의 공급방식에 따라 분류되는 유가식 배양방법이다. 구체적으로, 배지를 간헐적으로 공급하는 배양법으로써 배양액 중의 기질 농도를 임의로 제어할 수 있다. 기질은 적당한 속도로 첨가되며 유출이 없기 때문에 공급되는 기질의 양과 미생물에 의한 소비량 사이에 균형을 유지함으로써 기질을 자유롭게 제어할 수 있다. 본 발명에서, 상기 발효 공정은 30℃, 250 ~ 600rpm에서 수행되었고, 배양 종료시까지 pH 7.0이 유지되도록 하였으며, 공기 유입 속도와 최소 용존 산소는 각각 2vvm과 20% 공기 포화도로 유지하고 공기포화도 수준이 70%에 도달했을 때 배지가 공급되도록 하는 방법으로 수행되었으나, 구체적인 공정이 상기 조건으로 제한되는 것은 아니다.
또한, 본 발명은 하기 단계를 포함하는, 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 배지에서 배양하여 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 추출 및 수득하는 단계.
또한, 본 발명은 하기 단계를 포함하는, 빌리버딘 (Biliverdin)의 생산방법을 제공한다.
(a) 상기 재조합 미생물을 배지에서 배양하여 빌리버딘을 생성시키는 단계; 및
(b) 상기 생성된 빌리버딘을 추출 및 수득하는 단계.
본 발명에 있어서, 상기 헴을 포함한 세포 내 포르피린의 추출은 각각 아세톤-산 처리 방법을 통해 수행될 수 있고, 바람직하게 상기 아세톤-산 처리 방법의 산은 염화수소 (HCl)일 수 있으며, 더욱 바람직하게 아세톤-산 처리방법은 99% 아세톤과 1.6M 염화수소 (HCl) 혼합물이 95 : 5 비율로 혼합된 혼합물일 수 있다.
이하, 본 발명의 이해를 돕기 위하여 바람직한 실시예를 제시한다. 그러나 하기의 실시예는 본 발명을 보다 쉽게 이해하기 위하여 제공되는 것일 뿐, 하기 실시예에 의해 본 발명의 내용이 한정되는 것은 아니다.
[실시예]
실시예 1. AlaS, DtxR, HemE, HemY, HemH, HemQ, HrtBA, HmuO, CcsA 유전자의 확보
본 발명의 실시예에서, AlaS 유전자는 로도박터 캡슐라투스 (Rhodobacter capsulatus)의 genomic DNA에서 확보하였고, DtxR, HemE, HemY, HemH, HemQ, HrtB, HrtA, HmuO 및 CcsA 유전자는 모두 코리네박테리움 글루타믹쿰 (Corynebacterium glutamicum)의 genomic DNA로부터 확보하였다. 또한, lacI에 의해 발현이 조절되고 고발현 tac 프로모터를 가지는 pMT-tac 또는 pEKEx2 벡터로 상기 각 유전자들을 클로닝하기 위하여, 벡터의 해당 제한효소 서열을 포함하는 정방향 및 역방향 프라이머를 각각 디자인하였으며, 합성된 프라이머를 이용하여 중합효소연쇄반응 (PCR)을 수행하였다. 상기 각 유전자에 특이적으로 합성된 프라이머 서열은 하기 표 1에 나타내었다.
| 프라이머 | 서열 (5'→3') | 서열번호 |
| alaS_F | ATAGTCGACAAGGAGATATAGATGGACTACAATCTCGCGC | 17 |
| alaS_R | ATAGGATCCTCAGGCAGAGGCC | 18 |
| dtxR_F | ATAGGATCCAAGGAGATATAGATGAAGGATCTGG | 19 |
| dtxR_R | ATAGAGCTCTTAGCCCTCAACCTTTTCTACG | 20 |
| hemE_F | AAAAGGTTGAGGGCTAAGAGCTAAGGAGATATAGATGTGGCTTCTTTTCCTAAATTGGGA | 21 |
| hemE_R | CGACGGCCAGTGAATTCGAGCTCTTAAGAATGAATGATGGAGACGGCT | 22 |
| hemY_F | ATAGGATCCATGCGTTTTGCCATCATCG | 23 |
| hemY_R | ATAGGTACCTTATCCCAGCAACCTGTGTAC | 24 |
| hemY_F2 | TCACACAGGAGATATCATATCGATGCGTTTTGCCATCATCG | 25 |
| hemY_R2 | ATTCATGTATATCTCCTTATCGTTATCCCAGCAACCTGTGTAC | 26 |
| hemH_F | CCCATCGATAAGGAGATATACATGAATGAACGCACATCGGATGC | 27 |
| hemH_R | AAAGGATCCCTAGTTGGCAGCTGGCGC | 28 |
| hemQ_F | CACGGATCCATGAGCGAGCTCGATATTAAACAGC | 29 |
| hemQ_R | CCAGCGGCCGCTTAAGGAAGAACCTTAATCAGATCTGCAATG | 30 |
| hrtB_F | TCTTCCTTAAGCGGCCAAGGAGATATACATGTTTCAAGGACTAAAAGAAC | 31 |
| hrtA_R | GCCAAAACAGGCGGCCGCTACAGGGTGTGGGGTGTGA | 32 |
| ccsA_F | TCTTCCTTAAGCGGCCAAGGAGATATACATGTTGCCCGTAAACCAAACG | 33 |
| ccsA_R | GCCAAAACAGGCGGCCGCTTAGTTCAGTCCGGCGTA | 34 |
| cmR_F | CACCCCACACCCTGTAGCGGCCGCCTGTTTTGGCGG | 35 |
| cmR_R | ACTAGGAGAAGTTAATAAATACAATTACGCCCCGCCCTGC | 36 |
| hmuO_F | GTTCTTCCTTAAGCGGCCAAGGAGATATACATGACAAGCATTATTGCAAGCAACA | 37 |
| hmuO_R | CCGCCAAAACAGGCGGCCGCTTAAGCAAGAGCCTGAAAAACTTGC | 38 |
PCR 수행 결과, 1230bp의 AlaS 유전자, 687bp의 DtxR 유전자, 1125bp의 HemE 유전자, 1347bp의 HemY 유전자, 1113bp의 HemH 유전자, 699bp의 HemQ 유전자, 1680bp의 HrtBA 유전자, 648bp의 HmuO 및 1026bp의 CcsA 유전자를 각각 확보하였다. 상기 각 유전자들이 암호화하는 단백질의 아미노산 서열은 서열번호 3 내지 12로 나타내었다.
실시예 2. 확보된 유전자 및 HemA, HemL을 각각 포함하는 재조합 벡터 및 재조합 미생물 제작
본 발명자들은 상기 실시예 1을 통해 확보된 유전자인 AlaS, DtxR, HemE, HemY, HemH, HemQ, HrtBA, HmuO 및 CcsA에 더하여 HemA 및 HemL 유전자를 단일 또는 조합으로 포함하는 재조합 벡터를 제조하고, 상기 벡터를 도입한 재조합 미생물을 제작하고자 하였다.
상기 각 유전자를 포함하는 재조합 벡터를 구축하기 위한 목표 유전자, 벡터, 프라이머, 제한효소 부위 및 클로닝 방법은 하기 표 2에 정리하여 나타내었다.
| 타겟 벡터 | 도입 유전자 | 억셉터 벡터 | 프라이머 | 제한효소 | 클로닝 방법 |
| pX2-S | alaS | pEKEx2 | alaS_F | SalI | T4 DNA Ligation |
| pX2-ALS | pX2-AL | alaS_R | BamHI | ||
| pX2-ALSDt | dtxR | pX2-ALS | dtxR_F | BamHI | T4 DNA Ligation |
| dtxR_R | SacI | ||||
| pX2-ALSDtE | hemE | pX2-ALSDt | hemE_F | SacI | Gibson assembly |
| hemE_FR | |||||
| pMTZ-Y | hemY | pMTZ | hemY_F | BamHI | T4 DNA Ligation |
| hemY_R | KpnI | ||||
| pMTZ-H | hemH | pMTZ | hemH_F | ClaI | T4 DNA Ligation |
| hemH_R | BamHI | ||||
| pMTZ-Q | hemQ | pMTZ and | hemQ_F | BamHI | T4 DNA Ligation |
| pMTZ-HQ | pMTZ-HQ | hemQ_R | NotI | ||
| pMTZ-YHQ | hemY | pMTZ-HQ | hemY_F2 | ClaI | Gibson assembly |
| hemY_R2 | |||||
| pMTC-YHQ | CmR | pMTZ-YHQ | cmR_F | NotI | T4 DNA Ligation |
| cmR_R | SnaBI | ||||
| pMTZ-YHQBA | hrtBA | pMTZ-YHQ | hrtB_F | NotI | Gibson assembly |
| hrtB_R | |||||
| pMTZ-YHQcA | ccsA | pMTZ-YHQ | ccsA_F | NotI | Gibson assembly |
| ccsA_R | |||||
| pMTC-YHQBA | CmR | pMTZ-YHQBA | cmR_F | NotI | T4 DNA Ligation |
| cmR_R | SnaBI | ||||
| pMTC-YHQO | hmuO | pMTC-YHQ | hmuO_F | NotI | T4 DNA Ligation |
| hmuO_R | SnaBI | ||||
| pMTC-HrtBA | hrtBA | pMTC | hrtB_F | Gibson assembly | |
| hrtA_R | |||||
| pJYS2_empty | pJYS2 fragment 1 | JYS2_F | Gibson assembly | ||
| JYS2_R | |||||
| pJYS2 fragment 2 | JYS2_F2 | ||||
| JYS2_R2 | |||||
| pJYS2_hrrS | crRNA | pJYS2_empty | hrrS_F | BamHI | Gibson assembly |
| Of hrrS | hrrS_R | ||||
| pJYS2_htaA | crRNA | pJYS2_empty | htaA_F | BamHI | Gibson assembly |
| Of htaA | htaA_R | ||||
| pJYS2_hmuT | crRNA | pJYS2_empty | hmuT_F | BamHI | Gibson assembly |
| Of hmuT | hmuT_R | ||||
| pJYS2_hmuO | crRNA | pJYS2_empty | hmuO_F | BamHI | Gibson assembly |
| Of hmuO | hmuO_R | ||||
| pJYS2_ldh | crRNA_ | pJYS2_empty | ldh_F | Gibson assembly | |
| ldh | ldh_R | ||||
상기 유전자 클로닝에서, 대장균의 배양은 5g/L 효모 추출물, 10g/L 트립톤 및 10g/L NaCl로 구성된 LB 배지를 사용하였다. 또한, 코리네박테리움 균주의 유전자 클로닝을 위한 배양은 3.7g/L BHI 배지, 9.1g/L 솔비톨 및 20g/L 글루코오스로 구성된 BHISG 배지에서 수행하였다. T4 DNA 라이게이션 (ligation)을 위해서는 적절한 제한효소 (New England Biolab)를 이용하여 삽입 DNA와 벡터 DNA를 절단한 다음, 혼합물 형태에서 T4 DNA ligase (Enzynomics)로 연결하였다. Gibson assembly는 삽입 DNA를 DpnI로 처리하고 벡터 DNA는 적절한 제한효소를 이용하여 절단한 후 혼합물 형태에서 Gibson assembly 키트 (New England Biolab)를 이용해 연결하였다. 재조합 벡터를 구축하기 위한 모든 실험은 제조업체의 지침에 따라 수행되었으며, 직접 제작하거나 공지된 본 실시예에서 사용된 모든 재조합 벡터를 하기 표 3에 정리하여 나타내었다. 이후 상기에서 구축된 재조합 벡터를 대장균 또는 코리네박테리움 글루타믹쿰으로 도입하여 균주를 형질전환시켰으며, 이를 통해 제조된 모든 재조합 미생물을 하기 표 4에 나타내었다.
| 재조합 벡터 | 특성 | 참조 |
| pEKEx2 | C. glutamicum-E. coli 셔틀 벡터 (shuttle vector), Ptac, lacI, KanR, pBL1 ori | (Ko et al., 2018) |
| pX2-AL | Salmonella typhimurium 유래 hemA M 유전자 및 E. coli 유래 hemL 유전자 전달용 pEKEx2 | (Seok et al., 2019) |
| pX2-S | Rhodobacter capsulatus 유래 alaS 유전자 전달용 pEKEx2 | - |
| pX2-ALS | hemA M , hemL 및 alaS 유전자 전달용 pEKEx2 | - |
| pX2-ALSDt | hemA M , hemL, alaS 및 dtxR 유전자 전달용 pEKEx2 | - |
| pX2-ALSDtE | hemA M , hemL, alaS, dtxR 및 hemE 유전자 전달용 pEKEx2 | - |
| pMTZ | C. glutamicum-E. coli 셔틀 벡터, Ptac, AmpR, ZeoR, pCG1 ori | (Seok et al., 2019) |
| pMTZ-Y | C. glutamicum 유래 hemY 유전자 전달용 pMTZ | - |
| pMTZ-H | C. glutamicum 유래 hemH 유전자 전달용 pMTZ | - |
| pMTZ-Q | C. glutamicum 유래 hemQ 유전자 전달용 pMTZ | - |
| pMTZ-HQ | C. glutamicum 유래 hemH 및 hemQ 유전자 전달용 pMTZ | - |
| pMTZ-YHQ | C. glutamicum 유래 hemY, hemH 및 hemQ 유전자 전달용 pMTZ | - |
| pMTZ-YHQBA | C. glutamicum 유래 hemY, hemH, hemQ, hrtB 및 hrtA 유전자 전달용 pMTZ | - |
| pMTZ-YHQcA | C. glutamicum 유래 hemY, hemH, hemQ 및 ccsA 유전자 전달용 pMTZ | - |
| pMTC | C. glutamicum-E. coli 셔틀 벡터, Ptac, AmpR, CmRR, pCG1 ori | - |
| pMTC-YHQBA | C. glutamicum 유래 hemY, hemH, hemQ, hrtB 및 hrtA 유전자 전달용 pMTC | - |
| pMTC-YHQO | C. glutamicum 유래 hemY, hemH, hemQ 및 hmuO 유전자 전달용 pMTC | - |
| pMTC-HrtBA | C. glutamicum 유래 hrtB 및 hrtA 유전자 전달용 pMTC | - |
| pJYS1Peftu | pBL1ts oriVC.glu. Knr pSC101 oriVE. coli PlacM-FnCpf1 Peftu-RecT | Addgene: 85546 |
| pJYS2_crtYf | rep oriVC.glu. Spr pMB1 oriVE. coli Pj23119-crRNA targeting crtYf This | Addgene:85544 |
| pJYS2_empty | pJYS2_crtYf deleting the crRNA of the crtYf gene for pJYS2 derivatives | - |
| pJYS2_hrrS | hrrS 유전자에 대한 crRNA이 삽입된 pJYS2_empty | - |
| pJYS2_htaA | htaA 유전자에 대한 crRNA이 삽입된 pJYS2_empty | - |
| pJYS2_hmuT | hmuT 유전자에 대한 crRNA이 삽입된 pJYS2_empty | - |
| pJYS2_hmuO | hmuO 유전자에 대한 crRNA이 삽입된 pJYS2_empty | - |
| pJYS2_ldh | ldh 유전자에 대한 crRNA이 삽입된 pJYS2_empty | - |
| 재조합 미생물 | 특성 | 참조 |
| 코리네박테리움 유래 | ||
| ATCC 13032 | L-glutamate 생산 균주 | KCTC 1445 |
| ATCC 13826 | L-glutamate 생산 균주 | KCTC 3017 |
| ATCC 13059 | L-glutamate 생산 균주 | KCTC 1447 |
| ATCC 14067 | L-glutamate 생산 균주 | KCTC 1738 |
| 13032 AL | C. glutamicum ATCC 13032, pX2 hemAL | - |
| 13826 AL | C. glutamicum ATCC 13826, pX2 hemAL | (Ko et al., 2018) |
| 13059 AL | C. glutamicum ATCC 13059, pX2 hemAL | - |
| 14067 AL (AL) | C. glutamicum ATCC 14067, pX2 hemAL | - |
| S | C. glutamicum ATCC 14067, pX2-S | - |
| ALS | C. glutamicum ATCC 14067, pX2-ALS | - |
| ALSdt | C. glutamicum ATCC 14067, pX2-ALSDt | - |
| ALSdtE | C. glutamicum ATCC 14067, pX2-ALSDtE | - |
| ALS-Y | pMTZ-Y가 도입된 ALS | - |
| ALS-H | pMTZ-H가 도입된 ALS | - |
| ALS-Q | pMTZ-Q가 도입된 ALS | - |
| ALS-HQ | pMTZ-HQ가 도입된 ALS | - |
| ALS-YHQ | pMTZ-YHQ가 도입된 ALS | - |
| ALSdtE | C. glutamicum ATCC 14067, pX2-ALSDt | - |
| ALSDt-Y | pMTZ-Y가 도입된 ALSDt | - |
| ALSDt-H | pMTZ-H가 도입된 ALSDt | - |
| ALSDt-Q | pMTZ-Q가 도입된 ALSDt | - |
| ALSDt-HQ | pMTZ-HQ가 도입된 ALSDt | - |
| ALSDt-YHQ | pMTZ-YHQ가 도입된 ALSDt | - |
| ALSDt-YHQBA | pMTZ-YHQBA가 도입된 ALSDt | - |
| ALSDt-YHQcA | pMTZ-YHQcA가 도입된 ALSDt | - |
| ALSdtE | C. glutamicum ATCC 14067, pX2-ALSDtE | - |
| ALSDtE-YHQBA | pMTZ-YHQBA가 도입된 ALSDtE | - |
| ALSDtE-YHQBA2 | pMTC-YHQBA가 도입된 ALSDtE | - |
| ALSDtE-YHQO | pMTC-YHQO가 도입된 ALSDtE | - |
| ALSDtE-BA | pMTC-HrtBA가 도입된 ALSDtE | - |
| ΔS | ATCC14067의 hrrS 넉아웃 (knockout) 변이체 | - |
| ΔSA | ΔS의 htaA 넉아웃 변이체 | - |
| ΔSAT | ΔSA의 hmuT 넉아웃 변이체 | - |
| ΔSATO | ΔSAT의 hmuO 넉아웃 변이체 | - |
| ΔS:: ALSDt-YHQBA | pX2-ALSDt 및 pMTZ-YHQBA가 도입된 ΔS | - |
| ΔSA:: ALSDt-YHQBA | pX2-ALSDt 및 pMTZ-YHQBA가 도입된 ΔSA | - |
| ΔSAT:: ALSDt-YHQBA | pX2-ALSDt 및 pMTZ-YHQBA가 도입된 ΔSAT | - |
| ΔSAT:: ALSDtE-YHQBA | pX2-ALSDtE 및 pMTZ-YHQBA가 도입된 ΔSAT | - |
| ΔSAT:: ALSDtE-YHQBA(c) | pX2-ALSDtE 및 pMTC-YHQBA가 도입된 ΔSAT | - |
| ΔSATO:: ALSDtE-YHQBA | pX2-ALSDtE 및 pMTZ-YHQBA가 도입된 ΔSATO | - |
| ΔLdh | ATCC14067의 ldh 넉아웃 변이체 | - |
| ΔLdh::ALSDtE | pX2-ALSDtE 및 pMTC가 도입된 ΔLdh | - |
| ΔLdh::ALSDtE-BA | pX2-ALSDtE 및 pMTC-HrtBA가 도입된 ΔLdh | - |
실시예 3. CRISPR 기술을 이용한 재조합 미생물의 세포벽 단백질 및 헴 분해 단백질 발현 억제
본 발명자들은 CRISPR 기술을 이용하여 상기 실시예 2에서 제조된 재조합 미생물의 세포벽 단백질 및 헴 분해 단백질의 발현을 억제시키고자 하였다.
이를 위해, 표적 유전자의 crRNA-Spacer 서열을 합성하였으며, ssODNs (single-stranded oligodeoxynucleotides) 합성을 위한 프라이머 정보는 상기 표 1에 나타내었다. 또한 CRISPR용 재조합 벡터를 구축하기 위한 목표 유전자 Spacer 서열, 벡터, 프라이머, 제한 효소 부위 및 클로닝 방법은 상기 표 2에서 확인할 수 있다. CRISPR 시스템을 도입하기 위한 pJYS1_Peftu 및 pJYS2_crtYf 벡터는 Addgene (미국)에서 구입하였고, CRISPR용 재조합 벡터의 구축 전에 상기 pJYS2_crtYf 벡터에서 crtYf 유전자의 Spacer 서열을 제거하였다. 구체적으로는 crtYf 유전자의 crRNA-Spacer 서열을 제외한 벡터 서열을 두개의 PCR 단편으로 확보한 후 Gibson assembly를 통해 연결하여 pJYS2_empty 벡터를 생성하였다. 상기 방법으로 구축된 모든 재조합 벡터는 상기 표 3에 나타내었다.
한편, HrrS, HtaA, HmuT, HmuO 및 Ldh 유전자의 crRNA-Spacer 서열 및 PAM 부위는 CRISPR RGEN tool Cas-Designer (http://www.rgenome.net/cas-designer/)를 이용해 설계하였으며, 사용된 CRISPR 기술용 프라이머 정보를 하기 표 5에 나타내었다. 또한 HrrS, HtaA, HmuT, Ldh 유전자가 암호화하는 단백질의 아미노산 서열은 서열번호 13 내지 16으로 나타내었다.
| 프라이머 | 서열 (5'→3') | 서열번호 |
| crRNA | ||
| hrrS_F | CTAGGTATAATGGATCGAATTTCTACTGTTGTAGATACAGCCTCGCTG | 39 |
| hrrS_R | TTTATTTAAATGGATCCCCACAACCAGCAGCGAGGCTGTATCTACAA | 40 |
| htaA_F | CTAGGTATAATGGATCGAATTTCTACTGTTGTAGATGGCAATCGTTCC | 41 |
| htaA_R | TTTATTTAAATGGATCGATGTAATTGCGGAACGATTGCCATCTACAAC | 42 |
| hmuT_F | CTAGGTATAATGGATCGAATTTCTACTGTTGTAGATGACGCACCCTTA | 43 |
| hmuT_R | TTTATTTAAATGGATCGACTACGGATGTAAGGGTGCGTCATCTACAAC | 44 |
| hmuO_F | CTAGGTATAATGGATCGAATTTCTACTGTTGTAGATTGAATGATCTGC | 45 |
| hmuO_R | TTTATTTAAATGGATCCTTCCCGGTGAGCAGATCATTCAATCTACAAC | 46 |
| ldh_F | CTAGGTATAATGGATCGAATTTCTACTGTTGTAGATGGCTGCGCCGGC | 47 |
| ldh_R | TTTATTTAAATGGATCTTGTCATTTGTGCCGGCGCAGCCATCTACAAC | 48 |
| Lagging strand | ||
| Lagging_hrrS | CGGAAGCACCCAGCCCCACAACCAGCAGCTAGGCTGTCAAAATGTGGATACTGTTGCGA | 49 |
| Lagging_htaA | GCCACGCCGGTTTGGATGTAATTGCGGAATTATTGCCTAAATCCCCAGTTCAGGGAGCC | 50 |
| Lagging_hmuT | AGGCCAAGCTAGCGGCGAGGACTACGGATTAAAGGGTGCGTCGAAAAGCGTTATTCATG | 51 |
| Lagging_hmuO | ATGCCTGCGCATCGAGCTTCCCGGTGAGCTAATCATTCATAAACGTTGAGTGCTCGGCC | 52 |
| Lagging_ldh1 | ACGCAGCCATGGTTGTCATTTGTGCCGGCTAAGCCCAAAAGCCAGGCGAGACCCGCCTC | 53 |
| Lagging_ldh2 | ATGGTTGTCATTTGTGCCGGCGCAGCCCAGTAGCCAGGCGAGACCCGCCTCCAGCTGGT | 54 |
| Lagging_ldh3 | ACGCAGCCATGGTTGTCATATGAGCAGGATAAGCCCACAAGCCAGGCGAGACCCGCCTC | 55 |
| Sequencing | ||
| hrrS_seq1 | ATGCAGTCAAGCCTAGATCG | 56 |
| hrrS_seq2 | CGTTGACGTTCCGCAGCAAT | 57 |
| htaA_seq1 | ATGAAACTTGCACCTCGTATGCGGA | 58 |
| htaA_seq2 | GCAACCAAATCCACAACTAGCTGCG | 59 |
| hmuT_seq1 | CCCGCTAACCAAAACAGCCAGTTCC | 60 |
| hmuT_seq2 | CCATCAGCATCCGTCAAAGACACAG | 61 |
| hmuO_seq1 | ATGACAAGCATTATTGCAAGCAACA | 62 |
| hmuO_seq2 | GGACATAGTGATGAGCAACCAAACG | 63 |
| pJYS2_seq_F | CACGCTGTCGGCAGAGAA | 64 |
| pJYS2_seq_R | TCACACCGCATATGAAGCTTAAGAGTTTGTAGAAACG | 65 |
| pJYS1_seq_F | GAGATCCTGTCCTCCGTGTG | 66 |
| pJYS1_seq_R | GGTCCTTCTTGATCTGCTCG | 67 |
| ldhseq1 | GCAACAATGACGGCGAGA | 68 |
| ldhseq2 | GGAGCTTTCGCAGGTGAA | 69 |
| etc. | ||
| JYS2_F | TAATGGATCCATTTAAATAAAACGAAAGGC | 70 |
| JYS2_R | GGCAAATAGGCAGGATTGAT | 71 |
| JYS2_F2 | TTATTTAAATGGATCCATTATACCTAGGACTG | 72 |
| JYS2_R2 | ATCAATCCTGCCTATTTGCC | 73 |
CRISPR 기술을 이용한 유전체 편집은 공지된 방법을 참고하여 하기 과정에 따라 수행하였다. 구체적으로, 극저온 (-80℃)에서 보관한 Competent 상태의 코리네박테리움 균주를 10분 동안 천천히 해동시켰다. 이어서 pJYS1_eftu (1㎍ 이상), pJYS2_목표 유전자 (1㎍ 이상) 및 ssODNs (9㎍ 이상)를 80㎕의 Competent 세포에 주입하였다. 이후 20분 동안 얼음에서 대기한 다음, 세포를 미리 냉각된 0.2cm 큐벳 (Bio-Rad, USA)으로 옮기고, 2.5kV의 전압과 200Ω의 저항값으로 전기천공법을 수행하였다. 이후 세포가 들어있는 큐벳에 솔비톨과 글루코오스가 함유된 BHI (Brain-heart infusion) 배지 (BHISG) 1ml를 즉시 넣은 후 46℃에서 6분 동안 열 충격 처리를 하였다. 이어서 30℃에서 2-3시간 동안 세포를 회복시킨 후, 카나마이신 (25mg/L)과 스펙티노마이신 (200mg/L)이 함유된 BHISG 배지 한천 플레이트에 접종하고 30℃에서 2-3일 동안 배양하였다.
이후 재조합 미생물의 유전자 편집 여부를 확인하기 위해 다음과 같이 colony PCR을 수행하였다. 이를 위해, 한 개의 콜로니를 확보한 후 상기 표 5에 기재된 시퀀싱 (Sequencing) 프라이머를 이용해 PCR을 수행하여 게놈 상의 유전자를 확보하였다. PCR 산물의 염기서열은 코스모젠텍이나 마크로젠사에 분석을 의뢰하여 유전자 편집 여부를 확인하였으며, 그 결과 각 재조합 미생물에서 목표 유전자의 편집 효율을 하기 표 6에 나타내었다.
|
표적
유전자 |
표적 균주 | crRNA | Lagging strand |
Colony
Forming Unit |
편집효율 | |
| 크기 (bp) | DNA (ug) | |||||
| hrrS | WT | crRNA_hrrS | 59 | 9.05 | 2.28 x 103 | 8/8 |
| htaA | WT | crRNA_htaA | 59 | 9.05 | 2.31 x 103 | 4/4 |
| htaA | S | crRNA_htaA | 59 | 9.05 | 2.25 x 102 | 2/2 |
| hmuT | WT | crRNA_hmuT | 59 | 12.6 | 6.09 x 103 | 2/2 |
| hmuT | SA | crRNA_hmuT | 59 | 12.6 | 1.15 x 104 | 2/2 |
| hmuO | SAT | crRNA_hmuO | 59 | 9.05 | 4.75 x 102 | 0/8 |
| hmuO | SAT | crRNA_hmuO | 59 | 18.13 | 2.75 x 102 | 2/5 |
| hmuO | SAT | crRNA_hmuO | 59 | 45.33 | 2.0 x 102 | 2/5 |
| hmuO | SAT | crRNA_hmuO | 59 | 90.66 | 1.25 x 102 | 3/3 |
| ldh | WT | crRNA_ldh1 | 1 | 59 | 1.30 x 102 | 0/20 |
| ldh | WT | crRNA_ldh2 | 2 | 59 | 6.25 x 10 | 0/20 |
| ldh | WT | crRNA_ldh3 | 3 | 59 | 3.75 x 10 | 2/3 |
이어서 CRISPR용 재조합 벡터가 제거된 균주를 얻기 위해 플라스미드 제거 (Curing)를 하기 3단계로 수행하였다. 1단계, 콜로니를 5ml의 BHISG가 들어있는 50ml 튜브에 접종하고 37℃에서 24시간 이상 배양하였다. 2단계, 상기 세포 배양액 일부를 BHISG 배지 한천 플레이트에 스트리킹하고 37℃에서 24시간 이상 배양하였다. 3단계, 상기 1단계를 반복 수행할 경우 재조합 벡터가 모두 완전히 제거되었다.
실시예 4. 재조합 코리네박테리움의 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘의 생산을 위한 배양 및 분석방법
4-1. 배지 및 배양방법
목적 산물의 생산을 위한 본 배양은 42g/L 3-morpholinopropanesulfonic acid (MOPS), 40g/L 포도당, 20g/L (NH4)2SO4, 5g/L 요소, 2g/L 효모 추출물, 1g/L KH2PO4, 1g/L K2HPO4, 250mg/L MgSO4 · 7H2O, 10mg/L FeSO4 · 7H2O, 10mg/L CaCl2, 1mg/L ZnSO4 · 7H2O, 0.31mg/L CuSO4 · 5H2O, 200μg/L 비오틴, 100μg/L MnSO4 · H2O 및 20μg/L NiCl2 · 6H2O이 포함된 변형된 CGXII 배지 (mCGXII 배지)에서 수행되었다. 단, 빌리버딘 생산을 위한 본 배양 시에는 나머지 조성은 동일하되 효모 추출물을 첨가하지 않은 CGXII 배지를 이용하였다.
또한, 질소 공급원의 최적화를 위해 하기와 같은 배지들을 테스트하였다. mCGXII-Y10 배지는 mCGXII 배지에 8g/L 효모 추출물을 첨가하여 제조하였다. mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca는 각각 mCGXII-Y10 배지에 10g/L (NH4)2SO4, NH4Cl, 트립톤 및 카제인가수분해물을 첨가하여 제조하였다. 유가식 발효를 위해, mCGXII 배지 및 mCGXII-Tr 배지에서는 42g/L MOPS를 제외하였다. 카나마이신 (25mg/L), 암피실린 (대장균의 경우 50mg/L), 클로람페니콜 (대장균의 경우 33mg/L, 코리네박테리움 글루타믹쿰의 경우 5mg/L), 스펙티노마이신 (대장균의 경우 50mg/L, 코리네박테리움 글루타믹쿰의 경우 200mg/L) 및/또는 제오신 (25mg/L)을 경우에 따라 배지에 첨가하였다. 또한 이소프로필 β-D-1-티오갈락토피라노사이드 (Isopropyl β-D-1-thiogalactopyranoside, IPTG) (1mM) 및 FeSO4 · 7H2O (20mg/L)를 플라스크 배양 8시간 및 12시간에 각각 첨가하고 유가식 발효를 진행하였다. 필요한 경우 10mg/L 에탐부톨 (ethambutol)을 첨가하였다. 유가식 발효를 위한 유입 용액 (Feeding solution)은 500g/L 글루코오스, 10g/L (NH4)2SO4, 10g/L 효모 추출물, 2g/L KH2PO4 및 2g/L K2HPO4로 구성되었다. 아연-포르피린 생산을 위한 에탐부톨 농도 최적화 실험은 5mg/L, 25mg/L, 50mg/L, 100mg/L의 에탐부톨이 첨가된 mCGXII-Tr 배지에서 수행하였다.
플라스크 배양은 하기 과정에 따라 수행되었다. 구체적으로, 극저온에서 보관된 모든 야생형 및 재조합 코리네박테리움을 BHISG 한천 플레이트에 스트리킹하고 30℃에서 24시간 동안 배양하였다. 이후 한 개의 콜로니를 20mL의 BHISG 배지에 접종하고 30℃, 200rpm에서 16시간 동안 전배양하였다. 전배양된 세포를 50mL의 mCGXII 배지 또는 질소 공급원 최적화 배지 (mCGXII-Y10, mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca 배지)가 포함된 250mL 진탕 플라스크 (baffled flask)에 광학밀도 (Optical density, OD) 600 파장값 1의 농도로 접종하였다. 이후 30℃, 200rpm에서 48시간 동안 진탕 배양하여 본 배양을 진행하였다. 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ 생산을 위한 배양 실험은 mCGXII-Tr 배지로 수행하였으며 이외 조건은 상기 조건과 동일하게 수행하였다.
유가식 발효는 하기와 같이 수행되었다. 극저온에서 보관된 모든 야생형 및 재조합 코리네박테리움을 BHISG 한천 플레이트에 스트리킹하고 30℃에서 24시간 동안 배양하였다. 이후 한 개의 콜로니를 20mL의 BHISG 배지에 접종하고 30℃, 200rpm에서 16시간 동안 전배양하였다. 첫 번째로 전 배양된 세포는 200mL의 BHISG 배지를 포함하는 1000mL 진탕 플라스크에 접종하여 30℃, 200rpm에서 16시간 동안 전배양하였고, 두 번째로 전배양된 세포는 2L mCGXII 배지 또는 mCGXII-Tr 배지를 함유하는 6L 발효기에 광학밀도 600 파장값 2의 농도로 접종하였다. 발효는 30℃, 250~600rpm 조건에서 수행되었으며, 28% NH4OH와 6M H2SO4를 사용하여 pH 7.0 조건을 배양 종료 시까지 유지하였다. 공기 유입 속도와 최소 용존 산소는 각각 2vvm과 20% 공기 포화도로 유지되도록 하였고, 생성된 거품은 Antifoam 204 (Sigma-Aldrich)를 사용하여 제거하였다. 유입 용액은 공기포화도 수준이 70%에 도달했을 때 자동 공급되었다. 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ 생산을 위한 유가식 발효 실험은 mCGXII-Tr 배지로 수행하였으며 이외 조건은 상기 조건과 동일하게 수행하였다.
4-2. 세포 성장 및 헴, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘의 생산 분석
세포 성장은 UV-vis 분광 광도계 (Mecasys Co., Ltd.)를 사용하여 광학밀도 600 파장값에서 측정하였고, 글루코오스 농도는 제조사의 지침에 따라 포도당 분석 키트 (Sigma-Aldrich)를 사용하여 측정하였다.
세포 내 헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘 측정을 위한 전처리과정은 하기 과정에 따라 수행되었다. 구체적으로, 배양액 1mL을 13000rpm에서 2분 동안 원심분리하고 상층액을 분리하여 세포만을 확보한 후 세포 펠렛에 산성 아세톤 완충액 1mL(99% 아세톤 : 1.6M HCl = 95 : 5 비율)을 첨가하여 세포 내 포르피린을 추출하였다. 이어서 상기 샘플을 약 30초 동안 볼텍싱 (Vortexing)한 다음, 13000rpm에서 2분 동안 원심분리하였다. 세포 추출에서 얻은 상층액은 1:1 비율로 0.1N NaOH와 혼합하여 중화하였다. 세포 외 헴, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 측정은 세포 배양액의 상층액을 0.1N NaOH와 1:1 비율로 혼합한 후 측정하였다.
헴, 코프로포르피린 Ⅲ, 우로포르피린 Ⅲ, 아연-코프로포르피린 Ⅲ, 아연-우로포르피린 Ⅲ 및 빌리버딘의 정량 분석은 고성능 액체 크로마토그래피 (HPLC) 시스템 (Waters Corporation)을 이용하여 실시하였다. 세포 내 아미노산 농도 측정을 위해 Fastprep 24 (MP biomedicals, USA)를 사용한 Bead beating으로 세포 펠렛을 파쇄되었다. 상등액 및 추출된 세포 내부 샘플은 AccQ-Tag 아미노산 분석 키트 (Waters)를 이용해 제조사의 프로토콜에 따라 유도체화 한 후 HPLC 시스템으로 분석하였다.
4-3. mRNA 발현수준 분석
재조합 코리네박테리움 균주의 mRNA 발현수준은 하기 과정에 따라 수행하였다. ALS, ALS-H 및 ALSdt-H 재조합 코리네박테리움의 mRNA 발현 수준을 확인하기 위해 상기 실시예 4의 플라스크 배양과 동일한 조건으로 실험을 진행하였고, 16시간 배양 후 샘플을 회수하였다. 총 RNA는 Hybrid-R prep kit (GeneAll)를 이용하여 제조업체의 지침에 따라 추출하였으며, 상기 추출된 RNA에 대하여 M-MLV 역전사 효소 (Bioneer)를 이용하여 제조사의 지침에 따라 cDNA를 합성하였다. 상기 합성된 cDNA에 대하여 제조업체의 지침에 따라 HiPi Real-Time PCR 2x Master Mix (SYBR green)를 이용해 CFX connect Real-Time PCR (Bio-Rad) 기기를 이용하여 mRNA 수준을 측정하였으며, ΔΔCt 방법으로 상대적 mRNA 수준을 분석하였다. 이때, 16S rRNA를 내부 표준 물질로 사용하였다. 본 mRNA 발현 분석에 사용된 모든 프라이머는 서열 정보는 하기 표 7에 나타내었다.
| 프라이머 | Sequence (5'→3') | 서열번호 |
| RT hemA F | GGAATACGATCAGCGAGCTT | 74 |
| RT hemA R | CTCGTGGCATGGACAAATCC | 75 |
| RT hemB F | CGATGACCTGCTGATTATGG | 76 |
| RT hemB R | GCCTGAGCAACAGCCATCTG | 77 |
| RT hemC F | GATGCTGTGATGCTCGCCTA | 78 |
| RT hemC R | GCGGACGGTTTCAGTGTCGT | 79 |
| RT hemD F | CGTGAAGTTCTGGGCAACGC | 80 |
| RT hemD R | CTTCGCTTCAATGCAGATGC | 81 |
| RT hemE F | GTTGCCTGAGTACAAGAAGG | 82 |
| RT hemE R | CAACGGCACCACAATGTCAG | 83 |
| RT hemH F | CCTTGACCTGTGTGGAATAC | 84 |
| RT hemH R | TTGGTTCAGGATTCCTACGC | 85 |
| RT hemL F | GCGGTTACACTCAGCGTTCC | 86 |
| RT hemL R | TAGTGTCAGAAGTCTGAGCG | 87 |
| RT hemQ F | GCACAGTGTTGGCACGAACA | 88 |
| RT hemQ R | TGGGTGAAGAAGCAAAGGAC | 89 |
| RT hemY F | AGGTGGAGTGATGGGTATTC | 90 |
| RT hemY R | GCGAAGACACCACAGTATCG | 91 |
| RT sdhA F | ACCACATGAACCTGGTCTCC | 92 |
| RT sdhA R | TGGTAGGTGAACGCCTTGAC | 93 |
| RT sdhB F | GAGCTGCTTGACCACGTAAA | 94 |
| RT sdhB R | CAGGCTTATTCTGGTCAGCG | 95 |
| RT sdhC F | GGTGGCTTCGTTCTTGTTCA | 96 |
| RT sdhC R | TCCGATCTCACGCAGGAACT | 97 |
| RT narG F | CCAGCAGATTTTCCTTCAGG | 98 |
| RT narG R | CATACACTTTCCACGAGCAG | 99 |
| RT narH F | ATAAATGGGAAGGCGGTTGG | 100 |
| RT narH R | CACGGCTCGTAGTAATCATC | 101 |
| RT narK F | GGATTTGATCTCTCAGCAGG | 102 |
| RT narK R | GACCAATTTGCGGGTTCCAA | 103 |
| RT sufB F | AACTATGGTTGGCACGACTC | 104 |
| RT sufB R | GCTGCTGAAGCATCCATTCT | 105 |
| RT sufD F | ATTTCCCTACGCCGTCTTCG | 106 |
| RT sufD R | CAGTCGAGCATCGTCCTTTG | 107 |
| RT acn F | CATGGAGAAGCTGCCGTACT | 108 |
| RT acn R | GGTGAACTGGATTTCGATGC | 109 |
실시예 5. 헴 합성 경로 관련 유전자가 도입된 재조합 코리네박테리움 균주의 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산 수준 측정 및 분석
본 발명자들은 본 실시예에서 확보한 재조합 코리네박테리움 균주들의 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산량을 측정 및 비교 분석하기 위해, 먼저 야생형 코리네박테리움 글루타믹쿰 (WT), S (alaS 유전자 도입), AL (hemA 및 hemL 유전자 도입) 및 ALS (hemA, hemL 및 alaS 유전자 도입) 재조합 균주에서 헴 생산 수준을 측정하였다.
그 결과, 도 1에 나타낸 바와 같이 야생형 균주와 비교할 때 상기 3 종류의 재조합 균주에서 전구물질인 글루탐산 (Glutamate)과 글리신 (Glycine)의 소모와 함께 헴 (Heme) 생산 및 중간물질인 5-아미노레불린산 (ALA), 코프로포르피린 Ⅲ (CP Ⅲ), 우로포르피린 Ⅲ (UP Ⅲ)의 생산이 증가하는 것으로 나타났다. 더욱이, 그중에서도 C4 경로와 C5 경로를 통합한 ALS 재조합 균주에서 5-아미노레불린산의 생산이 현저히 증가하였으며, 헴 및 다른 전구물질들도 가장 높은 수준으로 생산이 증가하는 것을 확인하였다.
상기 결과에 근거하여, 본 발명자들은 ALS 재조합 균주에 코프로포르피린 Ⅲ 의존성 경로에 관여하는 코프로포르피리노겐 Ⅲ 산화효소 (HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (HemH) 및 과산화수소 의존성 헴 합성효소 (HemQ)를 각각 암호화하는 유전자 및 디프테리아 톡신 리프레서 (DtxR)를 암호화하는 유전자를 단일 또는 조합하여 추가적으로 도입한 하기 재조합 균주들에서 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산 수준을 측정하고자 하였다.
먼저, ALS 재조합 균주에 hemY, hemH 및 hemQ 유전자를 각각 또는 조합하여 도입한 재조합 균주 (ALS-Y, ALS-H, ALS-Q, ALS-HQ 및 ALS-YHQ)에서 상기 물질들의 생산을 측정하였다. 그 결과, 도 2a에서 볼 수 있는 바와 같이 ALS-Q 재조합 균주의 경우에만 ALS 균주 보다 약간 증가된 헴 (Heme) 생산을 나타내었을뿐, 다른 재조합 균주들에서는 헴 생산 및 전구물질인 코프로포르피린 Ⅲ (CP Ⅲ), 우로포르피린 Ⅲ (UP Ⅲ)의 생산이 감소하였다.
다음으로, 상기 재조합 균주들에서 dtxR 유전자가 함께 도입된 균주 (ALS-dtY, ALSdt-H, ALSdt-Q, ALSdt-HQ 및 ALSdt-YHQ)의 생산능력을 분석하였다. 그 결과, 도 2b에서 볼 수 있는 바와 같이 HemY, HemH 및 HemQ가 동시에 과발현과 함께 DtxR의 과발현이 성공적으로 헴 생산을 증가시키는 것을 확인하였다. 이러한 결과는 도 2c의 mRNA 발현 수준 측정 결과를 통해, 디프테리아 톡신 리프레서가 헴 생산 과정 중 발생하는 저해 요소를 해소해주는 것을 알 수 있었다.
실시예 6. 세포벽이 개량된 재조합 코리네박테리움 균주의 헴, 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ의 생산 및 외분비 수준 측정 및 분석
본 발명자들은 상기 재조합 코리네박테리움 균주에서 헴 생산량이 현저히 증가되는 것을 확인하였는바, 헴이 세포 외부로도 높은 수준으로 분비되는지를 검증하고자 하였다. 이를 위해 하기 방법에 따라 코리네박테리움 균주에서 세포벽에 대한 헴 결합 테스트를 수행하였다.
구체적으로, 극저온에서 보관된 각 코리네박테리움 균주를 BHISG 한천 플레이트에 스트리킹하고 30℃에서 24시간 동안 배양하였다. 이후 한 개의 콜로니를 20mL BHISG 배지 또는 10mg/L의 에탐부톨이 보충된 20mL의 BHISG 배지에 접종하고 30℃, 200rpm에서 16시간 동안 전 배양하였다. 이후 전 배양된 세포를 1mL의 mCGXII 배지를 포함하는 1.5mL 튜브에 광학밀도 600 파장값 5의 농도로 접종하였다. 접종 즉시 10mg/L 헤민 (hemin)을 튜브에 넣고 10초 동안 볼텍싱하여 혼합한 후 세포를 13000rpm에서 2분 동안 원심분리하였다. 상등액과 세포 펠렛은 앞서 언급한 전처리 방법과 동일한 방식으로 수행한 후 HPLC로 분석하여 헤민의 소재를 확인하였다. 그 결과, 하기 표 8에서 볼 수 있는 바와 야생형 코리네박테리움 균주의 경우 세포 내에서 생성되어 외부로 분비되는 헴의 86.91%가 세포벽에 결합하는 것을 확인하였다.
이에 본 발명자들은 도 3a에 도시된 바와 같이 코리네박테리움 균주의 세포벽 단백질과 헴의 결합을 저해하고자 하였으며, 이를 위해 상기 실시예 3에 기재된 바에 따라 ΔS (hrrS 유전자넉아웃), ΔSA (hrrS 및 htaA 유전자 넉아웃), 및 ΔSAT (hrrS, htaA 및 hmuT 유전자 넉아웃) 재조합 균주를 제조하고, 상기 방법과 동일하게 상기 재조합 균주들에서 헴의 세포벽 결합율을 측정하였다. 그 결과, 하기 표 8에서 볼 수 있는 바와 같이 ΔSAT 재조합 코리네박테리움 균주에서 헴의 세포벽 결합율이 가장 낮게 측정되었으며, 더욱이 배지에 에탐부톨을 첨가한 후 배양하였을 때 상기 결합율이 현저히 감소하는 것을 확인하였다.
| 균주 | DCW (g l -1 ) |
세포벽 결합 헴
(mg g DCW -1 ) |
결합/비결합 비율
a
(%) |
| WT | 1.71 | 4.28 ± 0.05 | 86.91 |
| ΔS | 1.58 | 4.22 ± 0.20 | 83.45 |
| ΔSA | 1.51 | 3.93 ± 0.29 | 75.26 |
| ΔSAT | 1.49 | 3.41 ± 0.35 | 72.51 |
| WT (ETB) | 1.48 | 3.27 ± 0.12 | 44.89 |
| ΔSAT (ETB) | 1.45 | 2.70 ± 0.12 | 36.83 |
a 세포벽 결합/비결합 비율: [세포벽 결합 헴]/[세포벽 결합 헴 + 비결합 헴] x 100
상기 결과에 근거하여, 본 발명자들은 상기 실시예 5에서 헴 생산을 가장 성공적으로 증가시킨 ALSdt-YHQ 재조합 균주를 기준으로 하여 헴 외분비 단백질인 HrtBA를 과발현하도록 형질전환된 ALSdt-YHQBA (ALSdt-YHQ 균주에 hrtBA 도입) 균주에서 헴의 외분비 (secreted heme) 수준을 분석하였다. 그 결과, 도 3b에 나타낸 바와 같이 HrtBA의 과발현에 의해 헴의 외분비가 증가하였으며, 에탐부톨이 포함된 배지에서 배양한 경우 헴의 세포외 생산이 더욱 증가한 것으로 나타났다. 이에 더하여, 상기 ALSdt-YHQBA 재조합 균주에 세포벽 단백질 발현을 함께 저해시킨 재조합 균주 (ΔS::ALSdt-YHQBA, ΔSA::ALSdt-YHQBA 및 ΔSAT::ALSdt-YHQBA)의 경우 헴의 세포 외분비가 더욱 증가하였고, 역시 에탐부톨이 포함된 배지에서 그 수준이 더 증진되는 것을 확인하였다.
한편, 특이하게도 도 4에서 볼 수 있는 바와 같이 헴 외분비 단백질을 과발현시킨 재조합 균주를 에탐부톨 첨가 하에 배양한 경우, 헴 외분비 증대와 함께 우로포르피린 Ⅲ의 외분비 증대가 확인되었다. 이러한 결과를 개선하기 위해, 본 발명자들은 ΔSAT::ALSdt-YHQBA 재조합 균주에 추가로 hemE 유전자를 도입하여 우로포르피리노겐 Ⅲ 디카복실레이즈 (HemE)를 과발현하는 재조합 균주 (ΔSAT::ALSdtE-YHQBA)를 제조하였고, 상기 재조합 균주의 경우 도 3b에서 볼 수 있는 바와 같이 에탐부톨 첨가 하에 배양 시 우로포르피리노겐 Ⅲ의 외분비가 거의 증대되지 않으면서 가장 높은 헴의 세포외 생산능을 갖는 것을 확인하였다.
실시예 7. 재조합 코리네박테리움 균주의 배양 조건 최적화
먼저, 본 발명자들은 상기 실시예 6의 결과에서 확인된 헴의 세포외 생산능이 가장 높은 ΔSAT::ALSDtE_YHQBA 균주를 이용하여, 헴 생산을 가장 효율적으로 높일 수 있는 최적의 배지 내 질소 공급원을 테스트하고자 하였다. 이를 위해 상기 실시예 4에 기재된 바와 같이 mCGXII 배지에 효모 추출물을 첨가한 mCGXII-Y10 배지 및 상기 mCGXII-Y10에 각각 (NH4)2SO4, NH4Cl, 트립톤 및 카제인가수분해물을 첨가한 mCGXII-AS, mCGXII-AC, mCGXII-Tr 및 mCGXII-Ca 배지를 이용하여 상기 ΔSAT::ALSDtE_YHQBA 균주와 ΔSAT::ALSDtE_YHQBA2 균주 (클로람페니콜 항생제 저항성 ΔSAT::ALSDtE_YHQBA 균주)를 배양하였다. 그 결과, 도 5에서 볼 수 있는 바와 같이 mCGXII-Tr 배지 조건에서 배양한 경우 상기 재조합 균주에 의한 헴 생산이 가장 높게 측정되었다. 따라서 상기 결과를 통해 트립톤이 본 발명에 따른 재조합 균주의 헴 생산능을 높일 수 있는 가장 최적의 질소원임을 알 수 있었다.
나아가 본 발명자들은 각각 mCGXII 배지, mCGXII에 에탐부톨이 첨가된 배지 (mCGXII + ETB), mCGXII-Tr 배지를 이용하여 ΔSAT::ALSDtE_YHQBA 균주와 ΔSAT::ALSDtE_YHQBA2 균주를 48시간 동안 유가식 배양을 진행하면서 글루코오스 (Glucose) 소비, 균주 성장 (Cell growth), 헴 외분비 및 총 헴 생산량을 배양 시간에 따라 측정하였다. 그 결과, 도 6에 나타낸 바와 같이 ΔSAT::ALSDtE_YHQBA2 균주를 mCGXII-Tr 배지에서 유가식 발효시킨 경우 각각 mCGXII 배지 및 mCGXII에 에탐부톨이 첨가된 배지에서 유가식 발효시킨 경우 보다 더 높은 헴 생산량이 달성되었으며, 더욱이 가장 높은 헴의 세포외 생산량을 확인하였다.
이에 더하여, 본 발명자들은 추가적으로 생성된 헴의 분해를 억제하기 위해 상기 재조합 균주에서 추가적으로 hmuO 유전자를 넉아웃시켜 HmuO 단백질의 발현이 억제된 ΔSATO::ALSDtE-YHQBA 균주를 제조하고 ΔSAT::ALSDtE_YHQBA 균주와 각각 플라스크 배양한 후 헴 생산 수준을 측정하였다. 그 결과, 도 7에서 볼 수 있는 바와 같이 hmuO 유전자가 함께 넉아웃된 ΔSATO::ALSDtE_YHQBA 균주의 경우 총 헴 생산량 및 세포 성장이 모두 크게 감소하는 것으로 나타났다. 이를 통해 HmuO 단백질의 발현 억제는 헴 생산과 세포 성장에 부정적인 영향을 미치는 것을 알 수 있었다.
실시예 8. 재조합 코리네박테리움 균주의 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ 생산 측정 및 분석
다음으로, 본 발명자들은 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ 생산능이 증대된 재조합 코리네박테리움 균주를 얻고자 하였다. 이를 위해, ALSDtE 재조합 균주 및 상기 균주에서 포르피린의 생산량을 증가시키기 위하여 L-젖산 탈수소효소 (L-lactate dehydrogenase)를 암호화하는 ldh 유전자를 넉아웃시킨 ΔLdh::ALSdtE 균주 및 헴 외분비 단백질인 HrtBA의 발현을 증가시킨 ALSdtE-BA 균주를 mCGXY10-Tr 배지에서 각각 플라스크 배양하고 아연-코프로포르피린 Ⅲ (Zn-CP Ⅲ)와 아연-우로포르피린 Ⅲ (Zn-UP Ⅲ)의 생산 및 외분비량을 측정하였다.
그 결과, 도 8에 나타낸 바와 같이 ALSDtE 균주를 배양한 경우 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ의 생산량이 가장 높은 것으로 나타났으며, ΔLdh::ALSdtE 및 ALSdtE-BA 균주에서 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ의 생산과 외분비가 증가하지 않은 것을 확인하였다.
나아가 상기 ALSDtE 균주에서 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ의 생산 및 분비를 효과적으로 높일 수 있는 에탐부톨의 최적 농도를 선정하고자 하였다. 이를 위해, mCGXII-Tr 배지에 에탐부톨을 다양한 농도 (5, 25, 50, 100mg/L)로 첨가하여 배양한 후 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ의 생산량을 측정하였다. 그 결과, 도 9에 나타낸 바와 같이 에탐부톨을 25mg/L 농도로 첨가하여 배양한 경우 가장 높은 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ 생산량을 확인하였다. 또한, 도 10에서 볼 수 있는 바와 같이 ALSDtE 균주를 mCGXII-Tr 배지를 이용하여 유가식 발효공정을 진행한 결과 가장 높은 아연-코프로포르피린 Ⅲ와 아연-우로포르피린 Ⅲ 생산량을 달성하였다.
실시예 9. 재조합 코리네박테리움 균주의 빌리버딘 생산 측정 및 분석
본 발명자들은 마지막으로 재조합 코리네박테리움 균주의 빌리버딘 (Biliverdin) 생산능을 증대시키고자 하였다. 이를 위해 상기 실시예 7에서 확인한 결과에 근거하여 헴의 세포외 생산능이 가장 높은 ΔSAT::ALSDtE-YHQBA 재조합 균주에서 세포벽 단백질들과 헴 외분비 단백질인 HrtBA의 발현을 증가시키지 않은 ALSDtE-YHQ 균주에 추가적으로 hmuO 유전자를 도입하여 헴 분해를 통한 빌리버딘 생성에 관여하는 HmuO 단백질을 과발현하는 ALSDtE-YHQO 균주를 제작하였다. 이후 ALSDtE-YHQ 및 ALSDtE-YHQO 균주를 CGXII 배지에서 배양한 후 빌리버딘 생산량을 측정하였다.
그 결과, 도 11에서 볼 수 있는 바와 같이 ALSDtE-YHQ 균주의 경우 빌리버딘이 전혀 생성되지 않은 반면, HmuO 단백질을 과발현하는 ALSDtE-YHQO 균주에서 빌리버딘의 생산량이 현저히 증가된 것을 확인하였다.
상기 진술한 본 발명의 설명은 예시를 위한 것이며, 본 발명이 속하는 기술분야의 통상의 지식을 가진 자는 본 발명의 기술적 사상이나 필수적인 특징을 변경하지 않고서 다른 구체적인 형태로 쉽게 변형이 가능하다는 것을 이해할 수 있을 것이다. 그러므로 이상에서 기술한 실시예들은 모든 면에서 예시적인 것이며 한정적이 아닌 것으로 이해해야만 한다.
<110> Korea University Research and Business Foundation
<120> Recombinant microorganism having enhanced productivity of heme,
coproporphyrin III, uroporphyrin III, Zn-coproporphyrin III,
Zn-uroporphyrin III and biliverdin, and method of producing heme,
coproporphyrin III, uroporphyrin III, Zn-coproporphyrin III,
Zn-uroporphyrin III and biliverdin using the same
<130> DHP21-K124-P1
<150> KR 10-2021-0018908
<151> 2021-02-10
<160> 109
<170> KoPatentIn 3.0
<210> 1
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<213> HemA
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<213> HemY
<400> 6
Met Arg Phe Ala Ile Ile Gly Ala Gly Leu Ala Gly Leu Thr Ala Ala
1 5 10 15
Tyr Glu Ile His Lys Ala Asp Pro Thr Ala Gln Ile Asp Val Leu Glu
20 25 30
Ala Gly Glu Arg Ile Gly Gly Lys Leu Phe Thr Val Pro Phe Ala Ser
35 40 45
Gly Pro Thr Asp Ile Gly Ala Glu Ala Phe Leu Ala Ala Arg Ser Asp
50 55 60
Ala Val Glu Phe Phe Thr Glu Leu Gly Leu Ala Asp Ser Leu Val Ser
65 70 75 80
Pro Ser Ala Ala Lys Ser Gln Tyr Phe Ala Gly Gly Ala Leu His Ala
85 90 95
Phe Pro Ala Gly Gly Val Met Gly Ile Pro Ser Asn Pro Pro Ala Gly
100 105 110
Ala Gln Asp Thr Ala Phe Asp Trp Thr Pro Gly Gln Asp Ile Ser Val
115 120 125
Gly Ala Leu Val Arg Arg Gln Tyr Gly Asp Glu Ile Val Asp Thr Val
130 135 140
Val Ser Ser Leu Leu Gly Gly Val Tyr Ser Ser Thr Ala Asp Asp Leu
145 150 155 160
Gly Val Arg Ala Ser Val Pro Ala Leu Ala Ala Ala Leu Asp Gln Leu
165 170 175
Ala Glu Ala Gly Glu Pro Val Thr Leu Ser Ala Ala Val Lys Ala Val
180 185 190
Glu Ala Gln Arg Glu Ala Ala Lys Thr Thr Ser Glu Thr Arg Pro Val
195 200 205
Phe Gln Thr Phe Lys Gly Gly Tyr Ala Glu Leu Tyr Glu Ala Leu Ala
210 215 220
Glu Gln Cys Gly Ala Asp Ile His Leu Asp Ser Phe Val Ser Ala Ile
225 230 235 240
Thr Lys Asp Gly Glu Gly Phe Ala Ile Lys Gly Gly Gly Glu Gly Thr
245 250 255
Tyr Asp Lys Val Ile Leu Ala Val Pro Ala Pro Thr Ala Ala Val Leu
260 265 270
Leu Arg Asp Leu Ala Pro Ala Ala Ala Pro His Leu Arg Ala Ile Lys
275 280 285
Leu Ala Ser Ser Ala Val Val Gly Met Arg Phe Asp Ser Ser Glu Gly
290 295 300
Leu Pro Asp Asn Ser Gly Val Leu Val Ala Val Asn Glu Pro Gly Ile
305 310 315 320
Thr Ala Lys Ala Phe Thr Phe Ser Ser Lys Lys Trp Pro His Leu Glu
325 330 335
Ala Arg Gly Gly Ala Leu Val Arg Ala Ser Phe Gly Arg Leu Gly Asp
340 345 350
Glu Ala Ser Ala Arg Met Asp Glu Asp Leu Leu Val Asp Ala Ala Leu
355 360 365
Asp Asp Leu Leu Thr Ile Thr Gly Phe Asp Gly Arg Ala Ala Gly Leu
370 375 380
Gly Glu Ile Phe Val Gln Arg Trp Phe Gly Gly Leu Pro Ala Tyr Gly
385 390 395 400
Val Asp His Ile Ala Thr Val Ser Ala Ala Arg Ala Glu Ile Ala Ala
405 410 415
Val Pro Gly Val Glu Ala Ile Gly Ala Trp Ala Gly Gly Val Gly Val
420 425 430
Pro Ala Val Ile Ala Asp Ala Gln Ala Ala Val His Arg Leu Leu Gly
435 440 445
<210> 7
<211> 370
<212> PRT
<213> HemH
<400> 7
Met Asn Glu Arg Thr Ser Asp Ala Phe Asp Ala Leu Leu Val Leu Ser
1 5 10 15
Phe Gly Gly Pro Glu Gly His Glu Glu Val Arg Pro Phe Leu Glu Asn
20 25 30
Val Thr His Gly Arg Gly Ile Pro Pro Glu Arg Leu Asp Glu Val Ala
35 40 45
Val His Tyr His His Phe Gly Gly Ile Ser Pro Ile Asn Ala Leu Asn
50 55 60
Arg Glu Ile Ile Ala Asn Val Glu Lys Glu Leu Ala Ser Arg Asp His
65 70 75 80
Lys Leu Pro Val Tyr Phe Gly Asn Arg Asn Trp Lys Pro Phe Asp Asn
85 90 95
Glu Ala Ala Glu Gln Met Ala Asp Asp Gly Val Lys Asn Ala Leu Val
100 105 110
Leu Ala Thr Ser Ala Trp Gly Gly Tyr Ser Gly Cys Arg Gln Tyr Gln
115 120 125
Glu Asp Ile Gln Gly Met Ile Lys His Leu Glu Ser Gln Gly Gln Ser
130 135 140
Ile Thr Phe Thr Lys Leu Arg Gln Phe Tyr Asp His Pro Arg Phe Val
145 150 155 160
Ser Thr Met Ala Gln Leu Val Gln Asp Ser Tyr Ala Lys Leu Pro Asp
165 170 175
Glu Leu Arg Asp Glu Ala Arg Leu Val Phe Thr Ala His Ser Ile Pro
180 185 190
Leu Thr Ala Asp Asn Ala Ala Gly Thr Pro Glu Asp Gly Ser Leu Tyr
195 200 205
Ser Thr Gln Val Lys Glu Ala Ser Ala Leu Ile Ala Glu Ala Val Gly
210 215 220
Val Ser Asp Phe Asp Val Val Trp Gln Ser Arg Ser Gly Ser Pro His
225 230 235 240
Thr Pro Trp Leu Glu Pro Asp Ile Val Asp His Ala Val Glu Leu Asn
245 250 255
Glu Lys Gly Gln Lys Ala Leu Val Val Cys Pro Val Gly Phe Ile Ser
260 265 270
Asp His Met Glu Val Ile Trp Asp Leu Asp Ser Glu Leu Met Glu Glu
275 280 285
Ala Glu Lys Arg Asn Met Val Val Glu Arg Val Ala Thr Val Gly Pro
290 295 300
Thr Asp Glu Phe Ala Ala Leu Val Val Asp Leu Ile Glu Glu Ala Glu
305 310 315 320
Leu Lys Arg Val Ile Glu Arg Leu Gly Lys Leu Pro Ala Arg Gly Ser
325 330 335
Ser Val Asn Gly Ala Pro Cys Gly Asp Gly Cys Cys Gly Thr Ala Lys
340 345 350
His Lys Thr Ala Arg Val Asn Pro Asn Ala Arg Ser Ala Ala Pro Ala
355 360 365
Ala Asn
370
<210> 8
<211> 232
<212> PRT
<213> HemQ
<400> 8
Met Ser Glu Leu Asp Ile Lys Gln Leu Asn Lys Leu Gln Arg Tyr Ser
1 5 10 15
Gln Trp Ala Val Phe Arg Ala Ile Pro Gly Ala Leu Asp Asp Asp Arg
20 25 30
Thr Glu Val Thr Asp Gln Ala Ala Lys Phe Phe Ala Asp Leu Glu Ala
35 40 45
Glu Gly Lys Val Thr Val Arg Gly Ile Tyr Asn Ala Ser Gly Leu Arg
50 55 60
Ala Asp Ala Asp Tyr Met Ile Trp Trp His Ala Glu Glu Phe Glu Asp
65 70 75 80
Ile Gln Lys Ala Phe Ala Asp Phe Arg Arg Thr Thr Ile Leu Gly Gln
85 90 95
Val Ser Glu Val Phe Trp Ile Gly Asn Ala Leu His Arg Pro Ser Glu
100 105 110
Phe Asn Lys Ala His Leu Pro Ser Phe Ile Met Gly Glu Glu Ala Lys
115 120 125
Asp Trp Ile Thr Val Tyr Pro Phe Val Arg Ser Tyr Asp Trp Tyr Ile
130 135 140
Met Glu Pro Leu Lys Arg Ser Arg Ile Leu Arg Glu His Gly Gln Ala
145 150 155 160
Ala Val Glu Phe Pro Asp Val Arg Ala Asn Thr Val Pro Ala Phe Ala
165 170 175
Leu Gly Asp Tyr Glu Trp Val Leu Ala Phe Glu Ala Asp Glu Leu His
180 185 190
Arg Ile Val Asp Leu Met His Lys Met Arg Tyr Thr Glu Ala Arg Leu
195 200 205
His Val Arg Glu Glu Leu Pro Phe Ile Ser Gly Gln Arg Val Asp Ile
210 215 220
Ala Asp Leu Ile Lys Val Leu Pro
225 230
<210> 9
<211> 230
<212> PRT
<213> HrtA
<400> 9
Met Thr Leu His Val Ser Asn Leu Asn Leu Thr Val Ala Asp Gly Ser
1 5 10 15
Thr Ser Arg Thr Leu Leu Asn Asn Ile Thr Phe Asp Val Gln Pro Gly
20 25 30
Glu Val Val Gly Ile Thr Gly Pro Ser Gly Ser Gly Lys Ser Thr Leu
35 40 45
Leu Ala Val Leu Gly Cys Leu Gln Ser Ala Asp Ser Gly Thr Ala Thr
50 55 60
Leu Gly Asp Ile Asp Leu Leu Asn Pro Gln Asn Arg Ala Ala Leu Arg
65 70 75 80
Arg Asn His Leu Gly Ile Val Phe Gln Gln Pro Asn Leu Leu Pro Ser
85 90 95
Leu Thr Val Leu Asp Gln Leu Leu Leu Ile Pro Arg Leu Gly Arg Ile
100 105 110
Leu Pro Pro Ser Arg Ser Ala Arg Thr Gln His Lys Asp Lys Ala Leu
115 120 125
Ser Leu Leu Asn Ser Ile Gly Leu Gly Asp Leu Ala Lys Arg Lys Val
130 135 140
Ser Glu Leu Ser Gly Gly Gln Gln Ala Arg Val Asn Leu Ala Arg Ala
145 150 155 160
Leu Met Asn Ser Pro Lys Leu Leu Leu Val Asp Glu Pro Thr Ala Ala
165 170 175
Leu Asp Gln His Ser Ala Ser Glu Val Thr Glu Leu Ile Val Ser Met
180 185 190
Ala His Gln Tyr Asn Ala Pro Thr Leu Phe Val Ser His Asp Met Asp
195 200 205
Ala Val Asn Thr Leu Asp Arg Ser Ile Glu Leu Val Asp Gly His Leu
210 215 220
Leu Thr Pro His Thr Leu
225 230
<210> 10
<211> 319
<212> PRT
<213> HrtB
<400> 10
Met Phe Gln Gly Leu Lys Glu Leu Thr Ala Ala Lys Gly Arg Thr Leu
1 5 10 15
Leu Ile Thr Val Thr Val Gly Leu Ile Ala Val Leu Val Thr Phe Leu
20 25 30
Ser Ala Leu Thr Ala Gly Leu Gly His Gln Ser Val Ser Ala Leu Lys
35 40 45
Tyr Leu Ala Gly Asp Asn Glu Leu Ile Leu Ala Asp Ser Gly Ser Thr
50 55 60
Thr Leu Ser Ala Ser Thr Leu Ser Asp Gln Ala Val Ala Gln Leu Glu
65 70 75 80
Asp Glu Gly Ala Gln Met Leu Trp Gln Val Arg Asp Arg Val Ala Asp
85 90 95
Thr Pro Thr Met Leu Leu Asn Ser Pro Asp Leu Ala Pro Gly Glu Val
100 105 110
Ser Leu Pro Ala Glu Leu Ala Asp Ser Glu Leu Ala Thr Ala His Asp
115 120 125
Val Val Asp Ser Ser Asn Asp Leu Tyr Leu Asp His Leu Pro Val Val
130 135 140
Leu Met Asn Thr Ser Asp Leu Ala Ser Leu Ala Gln Val Arg Gly Val
145 150 155 160
Thr Gly Pro Ala Gly Ala Phe Ala Ser Asp Val Ala Pro Pro Ser Asp
165 170 175
Thr Val Ala Leu Ser Gly Ser Glu Arg Trp Asn Ala Ser Ala Ser Tyr
180 185 190
Gln Gly Glu Gln Met Ser Leu Asn Leu Met Ile Val Met Leu Tyr Val
195 200 205
Ile Ser Ala Leu Val Leu Gly Ala Phe Phe Thr Val Trp Thr Ile Gln
210 215 220
Arg Leu Arg Gly Ile Ala Ile Ser Ser Ala Leu Gly Ala Ala Arg Arg
225 230 235 240
Val Leu Ile Ala Asp Ala Leu Gly Gln Ala Ile Ile Val Leu Gly Ile
245 250 255
Gly Ile Thr Ala Gly Thr Leu Ile Thr Val Ile Ser Ala Phe Gly Met
260 265 270
Gly Val Ala Met Pro Val Val Ile Ser Ser Ser Thr Thr Leu Phe Pro
275 280 285
Ala Leu Ile Leu Ala Ala Ala Gly Leu Ile Gly Ala Ala Ile Ser Leu
290 295 300
Gly Pro Ile Leu Arg Val Glu Pro Arg Ser Ala Leu Met Asn Ala
305 310 315
<210> 11
<211> 215
<212> PRT
<213> HmuO
<400> 11
Met Thr Ser Ile Ile Ala Ser Asn Ser Asp Leu Ser Glu Ala Leu Arg
1 5 10 15
Thr His Thr Ala Gln Ala His Glu Glu Ala Glu His Ser Thr Phe Met
20 25 30
Asn Asp Leu Leu Thr Gly Lys Leu Asp Ala Gln Ala Phe Ile Lys Leu
35 40 45
Gln Glu Gln Ser Trp Leu Phe Tyr Thr Ala Leu Glu Ala Ala Ala Arg
50 55 60
Ala Cys Ala Glu Asp Ser Arg Ala Ala Gly Leu Leu Asp Pro Arg Leu
65 70 75 80
Glu Arg Lys Glu Thr Leu Glu Ala Asp Leu Asp Lys Leu His Glu Asn
85 90 95
Thr Thr Trp Arg Asp Asn Val Thr Ala Thr Ala Ala Thr Ala Ser Tyr
100 105 110
Val Glu Arg Leu Glu Ser Ile Glu Ala Ala Lys Asp Phe Pro Arg Leu
115 120 125
Val Ala His His Tyr Val Arg Tyr Leu Gly Asp Leu Ser Gly Gly Gln
130 135 140
Val Ile Ala Arg Leu Val Asn Arg Glu Tyr Gly Val Ser Glu Glu Ala
145 150 155 160
Leu Ser Phe Tyr Cys Phe Glu Asp Leu Gly Lys Leu Lys Pro Tyr Lys
165 170 175
Asp Asn Tyr Arg Ala Glu Leu Asp Ala Leu Glu Leu Thr Ala Glu Glu
180 185 190
Arg Ala Ala Leu Leu Asp Glu Ala Ser Asp Ala Phe Arg Phe Asn Gln
195 200 205
Gln Val Phe Gln Ala Leu Ala
210 215
<210> 12
<211> 337
<212> PRT
<213> CcsA
<400> 12
Met Leu Pro Val Asn Gln Thr Tyr Ala Gln Phe Ser Asp Thr Ala Phe
1 5 10 15
Val Ser Ala Tyr Ile Ile Tyr Val Leu Ala Leu Ile Leu Ser Leu Val
20 25 30
Tyr Tyr Val Lys Gln Gln Gly Thr Ile Asp Ala Arg Arg Glu Gln Thr
35 40 45
Arg Val Ser Glu Leu Val Gly Ala Gly Gly Ser Ala Asp Val Asp Thr
50 55 60
Asp Leu Pro Asp Asp Ile Ala Asp Gly Val Leu Ala Asp Glu Asp Leu
65 70 75 80
Ala Lys Arg Glu Glu Thr Ala Arg Lys Leu Ala Asn Met Thr Gln Ser
85 90 95
Leu Met Trp Leu Gly Val Met Val His Leu Val Ser Val Val Met Arg
100 105 110
Ala Leu Ser Ala Ser Arg Phe Pro Phe Gly Asn Leu Tyr Glu Tyr Ile
115 120 125
Leu Met Val Thr Leu Phe Ala Met Ile Gly Ala Val Leu Ile Leu Gln
130 135 140
Arg Pro Gln Phe Arg Val Val Trp Pro Trp Ile Leu Thr Pro Met Leu
145 150 155 160
Ala Leu Leu Phe Tyr Gly Gly Thr Gln Leu Tyr Ser Asp Ala Ala Pro
165 170 175
Val Val Pro Ala Leu Gln Ser Phe Trp Phe Pro Ile His Val Ser Ser
180 185 190
Val Ser Ile Gly Ala Ser Ile Gly Ile Val Ser Gly Ile Ala Ser Leu
195 200 205
Leu Tyr Leu Leu Arg Met Trp Gln Pro Lys Gly Lys Glu Lys Gly Phe
210 215 220
Phe Gly Ala Val Ala Lys Pro Leu Pro Ser Gly Lys Thr Leu Asp Asn
225 230 235 240
Leu Ala Tyr Lys Thr Ala Ile Trp Thr Val Pro Ile Phe Gly Leu Gly
245 250 255
Ile Ile Leu Gly Ala Ile Trp Ala Glu Ala Ala Trp Gly Arg Phe Trp
260 265 270
Gly Trp Asp Pro Lys Glu Thr Val Ser Phe Ile Thr Trp Val Leu Tyr
275 280 285
Ala Gly Tyr Leu His Ala Arg Ala Thr Ala Gly Trp Arg Asn Thr Asn
290 295 300
Ala Ala Trp Ile Asn Ile Leu Ala Leu Val Thr Met Ile Phe Asn Leu
305 310 315 320
Phe Phe Ile Asn Met Val Val Ser Gly Leu His Ser Tyr Ala Gly Leu
325 330 335
Asn
<210> 13
<211> 444
<212> PRT
<213> HrrS
<400> 13
Met Gln Ser Ser Leu Asp Arg Val Ser Glu Thr Gly Arg Asn Glu Leu
1 5 10 15
Asp Val Glu Thr Leu Val Lys Lys Gly Asn Gln Pro Gly Ala Thr Ser
20 25 30
Tyr Arg Asn Ser Ile His Ile Leu Thr Ala Ser Leu Leu Val Val Gly
35 40 45
Leu Gly Ala Ser Ala Arg Leu Thr Leu Pro Met Phe Ala Leu Ser Cys
50 55 60
Val Leu Leu Phe Val Trp Gly Phe Leu Tyr Phe Tyr Gly Ser Thr Lys
65 70 75 80
Arg Val Asp Leu Arg His Gly Met Gln Leu Gly Trp Leu Phe Val Leu
85 90 95
Thr Leu Val Trp Ile Phe Met Val Pro Ile Val Pro Val Ser Ile Tyr
100 105 110
Leu Leu Phe Pro Leu Phe Phe Leu Tyr Leu Gln Val Met Pro Asp Val
115 120 125
Arg Gly Ile Ile Ala Ile Leu Gly Ala Thr Ala Ile Ala Ile Ala Ser
130 135 140
Gln Tyr Ser Val Gly Leu Thr Phe Gly Gly Val Met Gly Pro Val Val
145 150 155 160
Ser Ala Ile Val Thr Val Ala Ile Asp Tyr Ala Phe Arg Thr Leu Trp
165 170 175
Arg Val Asn Asn Glu Lys Gln Glu Leu Ile Asp Gln Leu Ile Glu Thr
180 185 190
Arg Ser Gln Leu Ala Val Thr Glu Arg Asn Ala Gly Ile Ala Ala Glu
195 200 205
Arg Gln Arg Ile Ala His Glu Ile His Asp Thr Val Ala Gln Gly Leu
210 215 220
Ser Ser Ile Gln Met Leu Leu His Val Ser Glu Gln Glu Ile Leu Val
225 230 235 240
Ala Glu Met Glu Glu Lys Pro Lys Glu Ala Ile Val Lys Lys Met Arg
245 250 255
Leu Ala Arg Gln Thr Ala Ser Asp Asn Leu Ser Glu Ala Arg Ala Met
260 265 270
Ile Ala Ala Leu Gln Pro Ala Ala Leu Ser Lys Thr Ser Leu Glu Ala
275 280 285
Ala Leu His Arg Val Thr Glu Pro Leu Leu Gly Ile Asn Phe Val Ile
290 295 300
Ser Val Asp Gly Asp Val Arg Gln Leu Pro Met Lys Thr Glu Ala Thr
305 310 315 320
Leu Leu Arg Ile Ala Gln Gly Ala Ile Gly Asn Val Ala Lys His Ser
325 330 335
Glu Ala Lys Asn Cys His Val Thr Leu Thr Tyr Glu Asp Thr Glu Val
340 345 350
Arg Leu Asp Val Val Asp Asp Gly Val Gly Phe Glu Pro Ser Glu Val
355 360 365
Ser Ser Thr Pro Ala Gly Leu Gly His Ile Gly Leu Thr Ala Leu Gln
370 375 380
Gln Arg Ala Met Glu Leu His Gly Glu Val Ile Val Glu Ser Ala Tyr
385 390 395 400
Gly Gln Gly Thr Ala Val Ser Ala Ala Leu Pro Val Glu Pro Pro Glu
405 410 415
Gly Phe Val Gly Ala Pro Val Leu Ala Asp Ser Asp Ser Ser Ala Thr
420 425 430
Gly Glu Val Glu Leu Ser Ser Pro Thr Asp Asp Glu
435 440
<210> 14
<211> 616
<212> PRT
<213> HtaA
<400> 14
Met Lys Leu Ala Pro Arg Met Arg Met Arg Ser His Lys Thr Phe Ala
1 5 10 15
Ala Leu Ala Ser Leu Ala Leu Val Ile Gly Leu Gly Gln Val Pro Ile
20 25 30
Ala Lys Ala Asp Thr Glu Tyr Arg Thr Ala Ser Asp Gly Ser Leu Asn
35 40 45
Trp Gly Phe Arg Gln Ser Phe Arg Asn Tyr Ile Gln Thr Gly Val Ala
50 55 60
Lys Gly Ser Ile Met Leu Gly Asp Gly Ala Ser Asp Asn Gly Gly Asn
65 70 75 80
Phe Ala Phe Thr Pro Arg Thr Asn Gly Thr Thr Val Thr Ser Asp Ser
85 90 95
Gln Gly Thr Val Glu Phe Asn Gly Ser Val His Phe Leu Gly His Gln
100 105 110
Ala Asp Asp Lys Trp Ile Leu Asp Thr Thr Met Ser Asp Ile Lys Met
115 120 125
Val Phe Asn Gly Ser Ser Ala Gln Leu Val Val Asp Leu Val Ala Arg
130 135 140
Glu Phe Lys Gly Thr Thr Tyr Asp Asp Ile Gly Glu Tyr Ile Ile Ser
145 150 155 160
Asp Asp Ile Val Leu Ala Asp Val Ser Leu Asn Ser Ala Ala Asp Phe
165 170 175
Ser Gln Asp Ser Ile Asp Leu Ser Gly Thr Thr Ala Leu Thr Ala Ala
180 185 190
Gly Ala Gln Ala Phe Gly Gly Phe Tyr Glu Thr Gly Asp Ala Leu Asp
195 200 205
Pro Thr Gly Gly Ser Leu Thr Ile Ser Ser Thr Thr Thr Thr Pro Ser
210 215 220
Thr Gly Thr Thr Ser Thr Ser Ala Ser Thr Ser Gly Gly Thr Ala Asp
225 230 235 240
Cys Ser Ser Gly Ala Leu Gly Val Val Thr Thr Gly Thr Asn Asp Gly
245 250 255
Met Leu Gly Thr Ile Gln Glu Val Asn Asn Thr Phe Ala Ile Trp Asn
260 265 270
Asn Leu Ile Val Asn Thr Glu Arg Met Phe Cys Asn Ile Asp Thr Leu
275 280 285
Lys Ala Arg Phe Asp Thr Asp Asp Ser Ser Asp Ser Ala Thr Ser Ala
290 295 300
Thr Ser Gly Thr Thr Ala Ser Thr Gly Thr Thr Ala Ala Thr Thr Ala
305 310 315 320
Gly Thr Thr Gly Thr Thr Gly Thr Ala Ser Thr Ala Ser Gly Thr Pro
325 330 335
Gly Thr Ser Gly Thr Ser Gly Thr Ser Gly Thr Ala Ala Thr Val Ala
340 345 350
Gly Thr Thr Pro Thr Asp Asn Gly Val Cys Thr Ala Ser Gly Ser Leu
355 360 365
Gly Val Thr Gln Ala Ser Ser Gln Trp Gly Val Lys Ala Ser Phe Gln
370 375 380
Asn Tyr Ile Arg Gly Ser Ile Ala Asn Gly Ser Trp Thr Leu Asn Gly
385 390 395 400
Val Gly Phe Asp Asn Gln Gln Phe Gln Phe Ser Gly Asn Ser Gly Ala
405 410 415
Val Asp Ala Glu Asn Lys Thr Gly Ser Ile Asn Phe Pro Gly Ser Ile
420 425 430
His Phe Thr Gly His Gly Gly Ile Leu Asp Met Gln Ile Ala Asn Ile
435 440 445
Glu Ile Ser Phe Asn Gly Asn Ser Gly Glu Leu Ile Ala Asp Val Val
450 455 460
Ser Ser Asp Met Asp Gly Asn Ser Thr Asn Tyr Gly Arg Thr Val Val
465 470 475 480
Gly Thr Leu Asn Phe Ser Ala Leu Asn Val Ser Ala Thr Glu Ala Ser
485 490 495
Gly Ser Ala Ser Val Ser Leu Ser Gln Ser Gly Ser Gln Ala Phe Ala
500 505 510
Asp Phe Tyr Thr Pro Gly Thr Gln Leu Asp Pro Ile Ser Phe Ser Ala
515 520 525
Thr Leu Gly Gly Glu Ala Ser Cys Ala Thr Gly Ser Thr Ser Thr Thr
530 535 540
Gly Ala Ala Ala Thr Ala Asn Thr Asp Asn Thr Glu Gly Val Ala Gly
545 550 555 560
Glu Glu Ser Thr Thr Pro Ala Asn Gln Asn Ser Gln Phe Gln Ile Arg
565 570 575
Gln Ala Ala Ala Asp Ser Thr Gly Leu Asp Thr Thr Thr Thr Met Leu
580 585 590
Leu Ile Leu Ala Ala Phe Val Val Ala Gly Gly Ser Met Thr Arg Phe
595 600 605
Thr Val Gly Asn Pro Thr Gly Lys
610 615
<210> 15
<211> 359
<212> PRT
<213> HmuT
<400> 15
Met Asn Asn Ala Phe Arg Arg Thr Leu Thr Ser Val Val Leu Ala Ala
1 5 10 15
Ser Leu Ala Leu Thr Ala Cys Ala Ser Trp Asp Ser Pro Thr Ala Ser
20 25 30
Ser Asn Gly Asp Leu Ile Glu Glu Ile Gln Ala Ser Ser Thr Ser Thr
35 40 45
Asp Pro Arg Thr Phe Thr Gly Leu Ser Ile Val Glu Asp Ile Gly Asp
50 55 60
Val Val Pro Val Thr Asp Asn Ala Ser Pro Ala Leu Pro Val Ser Leu
65 70 75 80
Thr Asp Ala Asp Gly Asn Asp Val Val Val Glu Asp Val Ser Arg Ile
85 90 95
Leu Pro Leu Asp Leu Tyr Gly Thr Tyr Ser Lys Thr Ile Ala Gly Leu
100 105 110
Gly Leu Val Asp Asn Ile Val Gly Arg Thr Val Ser Ser Thr Glu Pro
115 120 125
Ala Leu Ala Asp Thr Glu Val Val Thr Thr Gly Gly His Thr Leu Asn
130 135 140
Ala Glu Ala Ile Leu Asn Leu His Pro Thr Leu Val Ile Ile Asp His
145 150 155 160
Ser Ile Gly Pro Arg Glu Val Ile Asp Gln Ile Arg Ala Ala Gly Val
165 170 175
Ala Thr Val Ile Met Ser Pro Gln Arg Ser Ile Ala Ser Ile Gly Asp
180 185 190
Asp Ile Arg Asp Ile Ala Ser Val Val Gly Leu Pro Glu Glu Gly Glu
195 200 205
Lys Leu Ala Glu Arg Ser Val Ala Glu Val Glu Glu Ala Ser Thr Val
210 215 220
Val Asp Glu Leu Thr Pro Glu Asp Pro Leu Lys Met Val Phe Leu Tyr
225 230 235 240
Ala Arg Gly Thr Gly Gly Val Phe Phe Ile Leu Gly Asp Ala Tyr Gly
245 250 255
Gly Arg Asp Leu Ile Glu Gly Leu Gly Gly Val Asp Met Ala Ala Glu
260 265 270
Lys Gly Ile Met Asp Leu Ala Pro Ala Asn Ala Glu Ala Leu Ala Glu
275 280 285
Leu Asn Pro Asp Val Phe Val Met Met Ser Glu Gly Leu Val Ser Thr
290 295 300
Gly Gly Ile Asp Gly Leu Met Glu Arg Pro Gly Ile Ala Gln Thr Thr
305 310 315 320
Ala Gly Gln Asn Gln Arg Val Leu Ala Leu Pro Asp Gly Gln Ser Leu
325 330 335
Ala Phe Gly Ala Gln Thr Gly Glu Leu Leu Leu Arg Ala Ser Arg Glu
340 345 350
Leu Tyr Val Gln Gly Gly Glu
355
<210> 16
<211> 314
<212> PRT
<213> Ldh
<400> 16
Met Lys Glu Thr Val Gly Asn Lys Ile Val Leu Ile Gly Ala Gly Asp
1 5 10 15
Val Gly Val Ala Tyr Ala Tyr Ala Leu Ile Asn Gln Gly Met Ala Asp
20 25 30
His Leu Ala Ile Ile Asp Ile Asp Glu Lys Lys Leu Glu Gly Asn Val
35 40 45
Lys Asp Leu Asn His Gly Val Val Trp Ala Asp Ser Arg Thr Arg Val
50 55 60
Thr Lys Gly Thr Tyr Ala Asp Cys Glu Asp Ala Ala Met Val Val Ile
65 70 75 80
Cys Ala Gly Ala Ala Gln Lys Pro Gly Glu Thr Arg Leu Gln Leu Val
85 90 95
Asp Lys Asn Val Lys Ile Met Lys Ser Ile Val Gly Asp Val Met Asp
100 105 110
Ser Gly Phe Asp Gly Ile Phe Leu Val Ala Ser Asn Pro Val Asp Ile
115 120 125
Leu Thr Tyr Ala Val Trp Lys Phe Ser Gly Leu Glu Trp Asn Arg Val
130 135 140
Ile Gly Ser Gly Thr Val Leu Asp Ser Ala Arg Phe Arg Tyr Met Leu
145 150 155 160
Gly Glu Leu Tyr Glu Val Ala Pro Ser Ser Val His Ala Tyr Ile Ile
165 170 175
Gly Glu His Gly Asp Thr Glu Leu Pro Val Leu Ser Ser Ala Thr Ile
180 185 190
Ala Gly Val Ser Leu Ser Arg Met Leu Asp Lys Asp Pro Glu Leu Glu
195 200 205
Gly Arg Leu Glu Lys Ile Phe Glu Asp Thr Arg Asp Ala Ala Tyr His
210 215 220
Ile Ile Asp Ala Lys Gly Ser Thr Ser Tyr Gly Ile Gly Met Gly Leu
225 230 235 240
Ala Arg Ile Thr Arg Ala Ile Leu Gln Asn Gln Asp Val Ala Val Pro
245 250 255
Val Ser Ala Leu Leu His Gly Glu Tyr Gly Glu Glu Asp Ile Tyr Ile
260 265 270
Gly Thr Pro Ala Val Val Asn Arg Arg Gly Ile Arg Arg Val Val Glu
275 280 285
Leu Glu Ile Thr Asp His Glu Met Glu Arg Phe Lys His Ser Ala Asn
290 295 300
Thr Leu Arg Glu Ile Gln Lys Gln Phe Phe
305 310
<210> 17
<211> 40
<212> DNA
<213> Artificial Sequence
<220>
<223> alaS_F
<400> 17
atagtcgaca aggagatata gatggactac aatctcgcgc 40
<210> 18
<211> 22
<212> DNA
<213> Artificial Sequence
<220>
<223> alaS_R
<400> 18
ataggatcct caggcagagg cc 22
<210> 19
<211> 34
<212> DNA
<213> Artificial Sequence
<220>
<223> dtxR_F
<400> 19
ataggatcca aggagatata gatgaaggat ctgg 34
<210> 20
<211> 31
<212> DNA
<213> Artificial Sequence
<220>
<223> dtxR_R
<400> 20
atagagctct tagccctcaa ccttttctac g 31
<210> 21
<211> 60
<212> DNA
<213> Artificial Sequence
<220>
<223> hemE_F
<400> 21
aaaaggttga gggctaagag ctaaggagat atagatgtgg cttcttttcc taaattggga 60
60
<210> 22
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hemE_R
<400> 22
cgacggccag tgaattcgag ctcttaagaa tgaatgatgg agacggct 48
<210> 23
<211> 28
<212> DNA
<213> Artificial Sequence
<220>
<223> hemY_F
<400> 23
ataggatcca tgcgttttgc catcatcg 28
<210> 24
<211> 30
<212> DNA
<213> Artificial Sequence
<220>
<223> hemY_R
<400> 24
ataggtacct tatcccagca acctgtgtac 30
<210> 25
<211> 41
<212> DNA
<213> Artificial Sequence
<220>
<223> hemY_F2
<400> 25
tcacacagga gatatcatat cgatgcgttt tgccatcatc g 41
<210> 26
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> hemY_R2
<400> 26
attcatgtat atctccttat cgttatccca gcaacctgtg tac 43
<210> 27
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> hemH_F
<400> 27
cccatcgata aggagatata catgaatgaa cgcacatcgg atgc 44
<210> 28
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> hemH_R
<400> 28
aaaggatccc tagttggcag ctggcgc 27
<210> 29
<211> 34
<212> DNA
<213> Artificial Sequence
<220>
<223> hemQ_F
<400> 29
cacggatcca tgagcgagct cgatattaaa cagc 34
<210> 30
<211> 42
<212> DNA
<213> Artificial Sequence
<220>
<223> hemQ_R
<400> 30
ccagcggccg cttaaggaag aaccttaatc agatctgcaa tg 42
<210> 31
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> hrtB_F
<400> 31
tcttccttaa gcggccaagg agatatacat gtttcaagga ctaaaagaac 50
<210> 32
<211> 37
<212> DNA
<213> Artificial Sequence
<220>
<223> hrtA_R
<400> 32
gccaaaacag gcggccgcta cagggtgtgg ggtgtga 37
<210> 33
<211> 49
<212> DNA
<213> Artificial Sequence
<220>
<223> ccsA_F
<400> 33
tcttccttaa gcggccaagg agatatacat gttgcccgta aaccaaacg 49
<210> 34
<211> 36
<212> DNA
<213> Artificial Sequence
<220>
<223> ccsA_R
<400> 34
gccaaaacag gcggccgctt agttcagtcc ggcgta 36
<210> 35
<211> 36
<212> DNA
<213> Artificial Sequence
<220>
<223> cmR_F
<400> 35
caccccacac cctgtagcgg ccgcctgttt tggcgg 36
<210> 36
<211> 40
<212> DNA
<213> Artificial Sequence
<220>
<223> cmR_R
<400> 36
actaggagaa gttaataaat acaattacgc cccgccctgc 40
<210> 37
<211> 55
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_F
<400> 37
gttcttcctt aagcggccaa ggagatatac atgacaagca ttattgcaag caaca 55
<210> 38
<211> 45
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_R
<400> 38
ccgccaaaac aggcggccgc ttaagcaaga gcctgaaaaa cttgc 45
<210> 39
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hrrS_F
<400> 39
ctaggtataa tggatcgaat ttctactgtt gtagatacag cctcgctg 48
<210> 40
<211> 47
<212> DNA
<213> Artificial Sequence
<220>
<223> hrrS_R
<400> 40
tttatttaaa tggatcccca caaccagcag cgaggctgta tctacaa 47
<210> 41
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> htaA_F
<400> 41
ctaggtataa tggatcgaat ttctactgtt gtagatggca atcgttcc 48
<210> 42
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> htaA_R
<400> 42
tttatttaaa tggatcgatg taattgcgga acgattgcca tctacaac 48
<210> 43
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuT_F
<400> 43
ctaggtataa tggatcgaat ttctactgtt gtagatgacg caccctta 48
<210> 44
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuT_R
<400> 44
tttatttaaa tggatcgact acggatgtaa gggtgcgtca tctacaac 48
<210> 45
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_F
<400> 45
ctaggtataa tggatcgaat ttctactgtt gtagattgaa tgatctgc 48
<210> 46
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_R
<400> 46
tttatttaaa tggatccttc ccggtgagca gatcattcaa tctacaac 48
<210> 47
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> ldh_F
<400> 47
ctaggtataa tggatcgaat ttctactgtt gtagatggct gcgccggc 48
<210> 48
<211> 48
<212> DNA
<213> Artificial Sequence
<220>
<223> ldh_R
<400> 48
tttatttaaa tggatcttgt catttgtgcc ggcgcagcca tctacaac 48
<210> 49
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_hrrS
<400> 49
cggaagcacc cagccccaca accagcagct aggctgtcaa aatgtggata ctgttgcga 59
<210> 50
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_htaA
<400> 50
gccacgccgg tttggatgta attgcggaat tattgcctaa atccccagtt cagggagcc 59
<210> 51
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_hmuT
<400> 51
aggccaagct agcggcgagg actacggatt aaagggtgcg tcgaaaagcg ttattcatg 59
<210> 52
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_hmuO
<400> 52
atgcctgcgc atcgagcttc ccggtgagct aatcattcat aaacgttgag tgctcggcc 59
<210> 53
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_ldh1
<400> 53
acgcagccat ggttgtcatt tgtgccggct aagcccaaaa gccaggcgag acccgcctc 59
<210> 54
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_ldh2
<400> 54
atggttgtca tttgtgccgg cgcagcccag tagccaggcg agacccgcct ccagctggt 59
<210> 55
<211> 59
<212> DNA
<213> Artificial Sequence
<220>
<223> Lagging_ldh3
<400> 55
acgcagccat ggttgtcata tgagcaggat aagcccacaa gccaggcgag acccgcctc 59
<210> 56
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> hrrS_seq1
<400> 56
atgcagtcaa gcctagatcg 20
<210> 57
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> hrrS_seq2
<400> 57
cgttgacgtt ccgcagcaat 20
<210> 58
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> htaA_seq1
<400> 58
atgaaacttg cacctcgtat gcgga 25
<210> 59
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> htaA_seq2
<400> 59
gcaaccaaat ccacaactag ctgcg 25
<210> 60
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuT_seq1
<400> 60
cccgctaacc aaaacagcca gttcc 25
<210> 61
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuT_seq2
<400> 61
ccatcagcat ccgtcaaaga cacag 25
<210> 62
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_seq1
<400> 62
atgacaagca ttattgcaag caaca 25
<210> 63
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> hmuO_seq2
<400> 63
ggacatagtg atgagcaacc aaacg 25
<210> 64
<211> 18
<212> DNA
<213> Artificial Sequence
<220>
<223> pJYS2_seq_F
<400> 64
cacgctgtcg gcagagaa 18
<210> 65
<211> 37
<212> DNA
<213> Artificial Sequence
<220>
<223> pJYS2_seq_R
<400> 65
tcacaccgca tatgaagctt aagagtttgt agaaacg 37
<210> 66
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> pJYS1_seq_F
<400> 66
gagatcctgt cctccgtgtg 20
<210> 67
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> pJYS1_seq_R
<400> 67
ggtccttctt gatctgctcg 20
<210> 68
<211> 18
<212> DNA
<213> Artificial Sequence
<220>
<223> ldhseq1
<400> 68
gcaacaatga cggcgaga 18
<210> 69
<211> 18
<212> DNA
<213> Artificial Sequence
<220>
<223> ldhseq2
<400> 69
ggagctttcg caggtgaa 18
<210> 70
<211> 30
<212> DNA
<213> Artificial Sequence
<220>
<223> JYS2_F
<400> 70
taatggatcc atttaaataa aacgaaaggc 30
<210> 71
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> JYS2_R
<400> 71
ggcaaatagg caggattgat 20
<210> 72
<211> 32
<212> DNA
<213> Artificial Sequence
<220>
<223> JYS2_F2
<400> 72
ttatttaaat ggatccatta tacctaggac tg 32
<210> 73
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> JYS2_R2
<400> 73
atcaatcctg cctatttgcc 20
<210> 74
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemA F
<400> 74
ggaatacgat cagcgagctt 20
<210> 75
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemA R
<400> 75
ctcgtggcat ggacaaatcc 20
<210> 76
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemB F
<400> 76
cgatgacctg ctgattatgg 20
<210> 77
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemB R
<400> 77
gcctgagcaa cagccatctg 20
<210> 78
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemC F
<400> 78
gatgctgtga tgctcgccta 20
<210> 79
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemC R
<400> 79
gcggacggtt tcagtgtcgt 20
<210> 80
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemD F
<400> 80
cgtgaagttc tgggcaacgc 20
<210> 81
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemD R
<400> 81
cttcgcttca atgcagatgc 20
<210> 82
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemE F
<400> 82
gttgcctgag tacaagaagg 20
<210> 83
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemE R
<400> 83
caacggcacc acaatgtcag 20
<210> 84
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemH F
<400> 84
ccttgacctg tgtggaatac 20
<210> 85
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemH R
<400> 85
ttggttcagg attcctacgc 20
<210> 86
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemL F
<400> 86
gcggttacac tcagcgttcc 20
<210> 87
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemL R
<400> 87
tagtgtcaga agtctgagcg 20
<210> 88
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemQ F
<400> 88
gcacagtgtt ggcacgaaca 20
<210> 89
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemQ R
<400> 89
tgggtgaaga agcaaaggac 20
<210> 90
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemY F
<400> 90
aggtggagtg atgggtattc 20
<210> 91
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT hemY R
<400> 91
gcgaagacac cacagtatcg 20
<210> 92
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhA F
<400> 92
accacatgaa cctggtctcc 20
<210> 93
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhA R
<400> 93
tggtaggtga acgccttgac 20
<210> 94
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhB F
<400> 94
gagctgcttg accacgtaaa 20
<210> 95
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhB R
<400> 95
caggcttatt ctggtcagcg 20
<210> 96
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhC F
<400> 96
ggtggcttcg ttcttgttca 20
<210> 97
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sdhC R
<400> 97
tccgatctca cgcaggaact 20
<210> 98
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narG F
<400> 98
ccagcagatt ttccttcagg 20
<210> 99
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narG R
<400> 99
catacacttt ccacgagcag 20
<210> 100
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narH F
<400> 100
ataaatggga aggcggttgg 20
<210> 101
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narH R
<400> 101
cacggctcgt agtaatcatc 20
<210> 102
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narK F
<400> 102
ggatttgatc tctcagcagg 20
<210> 103
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT narK R
<400> 103
gaccaatttg cgggttccaa 20
<210> 104
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sufB F
<400> 104
aactatggtt ggcacgactc 20
<210> 105
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sufB R
<400> 105
gctgctgaag catccattct 20
<210> 106
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sufD F
<400> 106
atttccctac gccgtcttcg 20
<210> 107
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT sufD R
<400> 107
cagtcgagca tcgtcctttg 20
<210> 108
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT acn F
<400> 108
catggagaag ctgccgtact 20
<210> 109
<211> 20
<212> DNA
<213> Artificial Sequence
<220>
<223> RT acn R
<400> 109
ggtgaactgg atttcgatgc 20
Claims (23)
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자가 도입된, 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물.
- 제1항에 있어서,
상기 재조합 미생물은 추가로 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된 것을 특징으로 하는, 재조합 미생물.
- 제1항 또는 제2항에 있어서,
상기 재조합 미생물은 HemA, HemL, AlaS, DtxR, HemE, HemY, HemH, HemQ 및 HrtAB를 암호화하는 유전자가 도입되고; 및
HrrS, HtaA 및 HmuT를 암호화하는 유전자의 발현이 억제되어 있는 것을 특징으로 하는, 재조합 미생물.
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자가 도입된, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물.
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈(Heme oxygenase, HmuO)를 암호화하는 유전자가 도입된, 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물.
- 제1항, 제4항 및 제5항 중 어느 한 항에 있어서,
상기 글루탐산 생성능을 가지는 미생물은 코리네박테리움 글루타믹쿰 (Corynebacterium glutamicum)인 것을 특징으로 하는, 재조합 미생물.
- 제1항, 제4항 및 제5항 중 어느 한 항에 있어서,
상기 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 디프테리아 톡신 리프레서(Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ), 헴 수송단백질 (heme regulated transporter A and B) 및 헴 옥시게네이즈(Heme oxygenase, HmuO)는 각각 서열번호 1 내지 11로 표시되는 아미노산 서열로 이루어진 것을 특징으로 하는, 재조합 미생물.
- 제2항에 있어서,
상기 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)은 각각 서열번호 13 내지 15로 표시되는 아미노산 서열로 이루어진 것을 특징으로 하는, 재조합 미생물.
- 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현이 억제된, 헴 (Heme)의 외분비능이 향상된 재조합 미생물.
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 수송단백질 (heme regulated transporter A and B, HrtAB)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자를 도입시키는 단계를 포함하는, 제1항 또는 제2항의 헴 (Heme), 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법.
- 제10항에 있어서,
상기 제조방법은 막결합 헴 단백질 히스티딘 키네이즈 (Histidine kinase HrrS), 세포표면 헴 수용체 단백질 (cell surface heme receptor, HtaA) 및 헴결합 세포질 단백질 (Hemin-binding periplasmic protein, HmuT)로 구성된 군에서 선택되는 1종 이상을 암호화하는 유전자의 발현을 억제시키는 단계를 추가로 포함하는 것을 특징으로 하는, 제조방법.
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR) 및 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 제4항의 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ) 생산능력이 향상된 재조합 미생물의 제조방법.
- 글루탐산 (glutamic acid) 생성능을 가지는 미생물에 글루타밀-tRNA 리덕테이즈 (glutamyl-tRNA reductase, HemA), 글루타메이트-1-세미알데하이드 아미노트랜스퍼레이즈 (glutamate-1-semialdehyde aminotransferase, HemL), 아미노레불린산 합성효소 (Aminolevulinic acid synthase, AlaS), 전사조절인자 디프테리아 톡신 리프레서 (Diphtheria toxin Repressor, DtxR), 우로포르피리노겐 Ⅲ 디카복실레이즈 (Uroporphyrinogen Ⅲ decarboxylase, HemE), 코프로포르피리노겐 Ⅲ 산화효소 (Coproporphyrinogen Ⅲ oxidase, HemY), 코프로포르피린 Ⅲ 페로킬라테이즈 (Coproporphyrin Ⅲ ferrochelatase, HemH), 과산화수소 의존성 헴 합성효소 (Hydrogen peroxide-dependent heme synthase, HemQ) 및 헴 옥시게네이즈 (Heme oxygenase, HmuO)를 암호화하는 유전자를 도입시키는 단계를 포함하는, 제5항의 빌리버딘 (Biliverdin) 생산능력이 향상된 재조합 미생물의 제조방법.
- 하기 단계를 포함하는, 헴 (Heme)의 생산방법:
(a) 제1항 또는 제2항의 재조합 미생물을 철 이온 (Fe2+)을 포함하는 배지에서 배양하여 헴을 생성시키는 단계; 및
(b) 상기 생성된 헴을 추출 및 수득하는 단계.
- 제14항에 있어서,
상기 단계 (a)에서 배지 내에 5 내지 100mg/L 농도의 에탐부톨 (ethambutol)이 추가로 포함된 것을 특징으로 하는, 생산방법.
- 제14항에 있어서,
상기 단계 (a)에서 배지 내에 질소원으로 트립톤 (Tryptone)이 포함된 것을 특징으로 하는, 생산방법.
- 제14항에 있어서,
상기 배양은 유가식 발효 공정으로 이루어지는 것을 특징으로 하는, 생산방법.
- 하기 단계를 포함하는, 코프로포르피린 Ⅲ (coproporphyrin Ⅲ, CP Ⅲ) 및 우로포르피린 Ⅲ (uroporphyrin Ⅲ, UP Ⅲ)의 생산방법:
(a) 제1항 또는 제2항의 재조합 미생물을 배지에서 배양하여 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 코프로포르피린 Ⅲ 및 우로포르피린 Ⅲ를 추출 및 수득하는 단계.
- 하기 단계를 포함하는, 아연-코프로포르피린 Ⅲ (Zn-coproporphyrin Ⅲ, Zn-CP Ⅲ) 및 아연-우로포르피린 Ⅲ (Zn-uroporphyrin Ⅲ, Zn-UP Ⅲ)의 생산방법:
(a) 제4항의 재조합 미생물을 아연 이온 (Zn2+)을 포함하는 배지에서 배양하여 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 생성시키는 단계; 및
(b) 상기 생성된 아연-코프로포르피린 Ⅲ 및 아연-우로포르피린 Ⅲ를 추출 및 수득하는 단계.
- 제19항에 있어서,
상기 단계 (a)에서 배지 내에 5 내지 100mg/L 농도의 에탐부톨 (ethambutol)이 추가로 포함된 것을 특징으로 하는, 생산방법.
- 제19항에 있어서,
상기 단계 (a)에서 배지는 질소원으로 트립톤 (Tryptone)이 포함된 것을 특징으로 하는, 생산방법.
- 제19항에 있어서,
상기 배양은 유가식 발효 공정으로 이루어지는 것을 특징으로 하는, 생산방법.
- 하기 단계를 포함하는, 빌리버딘 (Biliverdin)의 생산방법:
(a) 제5항의 재조합 미생물을 배지에서 배양하여 빌리버딘을 생성시키는 단계; 및
(b) 상기 생성된 빌리버딘을 추출 및 수득하는 단계.
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