KR20190015374A - 표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 융합 단백질 - Google Patents
표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 융합 단백질 Download PDFInfo
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Abstract
본 발명의 목적은 표적 RNA를 조절하는 방법을 개발하는 것이다. mRNA로부터의 단백질 발현량을 향상시키는 기능적 도메인; 및 표적 mRNA에 대하여, RNA 염기에 선택적으로 결합 또는 RNA 염기 서열에 특이적으로 결합할 수 있는 PPR 단백질을 포함하는 융합 단백질이 제공된다.
Description
본 발명은 표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 융합 단백질에 관한 것이다.
최근, 다양한 분석법으로 밝혀진 핵산-결합성 단백질 인자를 이용하여 관심 있는 서열에 결합시키는 기술이 확립되어 이용되고 있다. 이 서열 특이적인 결합을 이용함으로써 표적으로 하는 DNA 서열의 제거 또는 그 하류에 존재하는 단백질 암호화 유전자의 발현 억제(활성화 또는 불활성화)가 가능하다.
DNA에 작용하는 단백질 인자를 이용하는 기술로는 징크 핑거 뉴클레아제(ZFN), TAL 이펙터 뉴클레아제(TALEN), Crispr-cas9 등이 알려져 있으나, RNA에 특이적으로 작용하는 단백질 인자를 이용하는 기술의 개발은 여전히 한정되어 있다.
본 발명자들은 식물에서 주로 발견되는 단백질인 PPR 단백질(펜타트리코펩티드 반복(pentatricopeptide repeat, PPR) 모티프를 갖는 단백질)의 특성을 이용하여 표적 RNA의 서열에 대하여 특이적으로 결합할 수 있는 단백질의 설계 방법을 제안하였다(특허문헌 1).
특허문헌 1에 따른 개시에 있어서는, PPR 모티프가 RNA 결합 특성을 나타낼 때 기능하는 아미노산을 동정하고, PPR 모티프의 구조와 표적 염기와의 관계를 밝힘으로써, 임의의 서열 및 길이를 갖는 RNA에 결합할 수 있는 PPR 모티프를 가지는 단백질을 구축할 수 있었다. 그러나 특허문헌 1에 따른 기술을 이용하여 실제로 표적 RNA를 억제는 방법은 지금까지 밝혀진 적이 없었다.
본 발명자들은 PPR 단백질을 이용하여 표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 방법을 예의 검토한 결과, 소정의 기능적 도메인과 PPR 단백질의 융합 단백질이 표적 mRNA로부터의 단백질 발현량을 향상시킴을 확인하여 본 발명을 완성하기에 이르렀다.
즉, 본 발명의 일 구현예는 표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 융합 단백질에 관한 것으로, 상기 융합 단백질은
(A) mRNA로부터의 단백질 발현량을 향상시키는 1개 이상의 기능적 도메인; 및
(B) 표적 mRNA에 대하여 RNA 염기 선택적 또는 RNA 염기서열 특이적으로 결합할 수 있는 폴리펩티드 모이어티
를 포함하며,
상기 (B)의 폴리펩티드 모이어티가 식 1로 표시되는 30 내지 38개의 아미노산 길이의 폴리펩티드로 이루어지는 PPR 모티프를 1개 이상 포함하는 폴리펩티드 모이어티이고:
식에서,
Helix A는 12개의 아미노산 길이의, a-나선 구조를 형성할 수 있는 모이어티이고, 식 2로 표시되며,
식 2에서, A1 내지 A12는 각각 독립적으로 아미노산을 나타내고;
X는 존재하지 않거나, 또는 1 내지 9개의 아미노산 길이로 이루어지는 모이어티이고;
Helix B는 11 내지 13개의 아미노산 길이로 이루어지는 a-나선 구조를 형성할 수 있는 모이어티이고;
L은 2 내지 7개의 아미노산 길이의 식 3으로 표시되는 모이어티이고:
식 3에서, 각 아미노산은 C 말단측으로부터 "i"(-1), "ii"(-2)로 넘버링되고,
단, Liii 내지 Lvii는 존재하지 않을 수 있고,
A1, A4 및 Lii의 세 개의 아미노산 조합 또는 A4 및 Lii의 두 개의 아미노산 조합이 표적 mRNA의 염기 또는 염기 서열에 대응한다.
또한, 본 발명에 따른 일 구현예에서, 상기 (B)의 폴리펩티드 모이어티는 상기 PPR 모티프를 2 내지 30개 포함하며, 상기 복수의 PPR 모티프가 표적 mRNA의 염기 서열에 특이적으로 결합하도록 배열되는 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 상기 (B)의 폴리펩티드 모이어티는 상기 PPR 모티프를 5 내지 25개 포함하는 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 상기 (A)의 기능적 도메인은 상기 (B)의 폴리펩티드 모이어티의 N 말단측 및/또는 C 말단측에 결합되는 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 상기 (A)의 기능적 도메인은 리보솜을 mRNA로 유도하는 도메인, mRNA의 번역개시 또는 번역촉진과 관련된 도메인, mRNA의 핵외 이송(nuclear export)과 관련된 도메인, 소포체 막에 대한 결합과 관련된 도메인, 소포체 보유 신호(ER retention signal) 서열을 포함하는 도메인 및 소포체 신호 서열을 포함하는 도메인으로 이루어지는 군으로부터 선택되는 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 리보솜을 mRNA로 유도하는 도메인은 밀도 조절된 단백질(Density-regulated protein, DENR), 악성 T-세포 증폭된 서열 1(Malignant T-cell amplified sequence 1, MCT-1), 번역 제어된 종양 단백질(Translationally-controlled tumor protein, TPT1) 및 징크 핑거 CCCH-도메인(Zinc finger CCCH-domain, Lerepo4)로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 포함하는 도메인이고,
상기 mRNA의 번역개시 또는 번역촉진과 관련된 도메인은 eIF4E 및 eIF4G로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 mRNA의 핵 외로의 수송과 관련된 도메인은 스템-루프 결합 단백질(Stem -loop binding protein, SLBP)의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 소포체 막에 대한 결합과 관련된 도메인은 SEC61B, 트랜스로콘 관련 단백질 알파(Translocon associated protein(TRAP)-alpha), SR-알파, 시토크롬 b5 환원효소 3(Cytochrome b5 reductase 3, Dia1) 및 p180으로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 소포체 보유 신호(ER retention signal) 서열은 KDEL(KEEL) 서열을 포함하는 신호 서열이거나, 또는
상기 소포체 신호 서열은 MGWSCIILFLVATATGAHS(서열번호 22)를 포함하는 신호 서열인 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 상기 각각의 PPR 모티프에서의 A1, A4 및 Lii의 세 개의 아미노산 조합은;
PPR 모티프의 표적 염기가 A(아데닌)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 트레오닌, 아스파라긴), (페닐알라닌, 세린, 아스파라긴), (페닐알라닌, 트레오닌, 아스파라긴), (이소류신, 아스파라긴, 아스파르트산) 또는 (트레오닌, 트레오닌, 아스파라긴)이고;
PPR 모티프의 표적 염기가 G(구아닌)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (글루탐산, 글리신, 아스파르트산), (발린, 트레오닌, 아스파르트산), (리신, 트레오닌, 아스파르트산) 또는 (류신, 트레오닌, 아스파르트산)이고;
PPR 모티프의 표적 염기가 U(우라실)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 아스파라긴, 아스파르트산), (이소류신, 아스파라긴, 아스파라긴), (이소류신, 아스파라긴, 아스파르트산), (이소류신, 메티오닌, 아스파르트산), (페닐알라닌, 프롤린, 아스파르트산) 또는 (티로신, 프롤린, 아스파르트산)이거나; 또는
PPR 모티프의 표적 염기가 C(시토신)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 아스파라긴, 아스파라긴), (이소류신, 아스파라긴, 아스파라긴), (발린, 아스파라긴, 세린) 또는 (이소류신, 메티오닌, 아스파르트산)인 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 상기 각각의 PPR 모티프에서의 A4 및 Lii의 두 개의 아미노산 조합은;
PPR 모티프의 표적 염기가 A(아데닌)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (트레오닌, 아스파라긴), (세린, 아스파라긴) 또는 (글리신, 아스파라긴)이고;
PPR 모티프의 표적 염기가 G(구아닌)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (트레오닌, 아스파르트산) 또는 (글리신, 아스파르트산)이고;
PPR 모티프의 표적 염기가 U(우라실)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (아스파라긴, 아스파르트산), (프롤린, 아스파르트산), (메티오닌, 아스파르트산) 또는 (발린, 트레오닌)이거나; 또는
PPR 모티프의 표적 염기가 C(시토신)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (아스파라긴, 아스파라긴), (아스파라긴, 세린) 또는 (류신, 아스파르트산)인 것을 특징으로 한다.
또한, 본 발명에 따른 또 다른 구현예는 본 발명에 따른 융합 단백질을 암호화하는 핵산에 관한 것이다.
또한, 본 발명에 따른 또 다른 구현예는 본 발명에 따른 핵산을 포함하는 벡터(바람직하게는, 발현 벡터)에 관한 것이다.
또한, 본 발명에 따른 또 다른 구현예는 세포 내에서 표적 mRNA로부터의 단백질 발현량을 향상시키는 방법에 관한 것으로, 방법은
본 발명에 따른 융합 단백질 또는 본 발명에 따른 벡터를 준비하는 단계; 및
융합 단백질 또는 벡터를 세포 내로 도입하는 단계를 포함한다.
또한, 본 발명에 따른 일 구현예에서, 세포는 진핵 세포인 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 세포는 동물 세포인 것을 특징으로 한다.
또한, 본 발명에 따른 일 구현예에서, 동물 세포는 인간 세포인 것을 특징으로 한다.
위에 기술된 본 발명의 하나 이상의 특징을 임의로 조합한 발명 또한 본 발명의 범위에 포함된다.
[PPR 모티프 및 PPR 단백질]
달리 명시되지 않는 한, 본 발명에 사용된 용어 "PPR 모티프"는 웹상의 단백질 도메인 검색 프로그램으로 아미노산 서열을 해석할 때, Pfam에서 PF01535, Prosite에서 PS51375로 얻어지는 E 값이 소정의 값 이하(바람직하게는 E-03)인 아미노산 서열을 갖는 30 내지 38개의 아미노산으로 이루어지는 폴리펩티드를 말한다. 본 발명에 정의된 PPR 모티프를 구성하는 아미노산의 위치 번호는 실질적으로 PF01535로서 정의된 바와 같은 반면, PS51375의 아미노산의 위치로부터 2를 빼서 얻어진 수에 해당한다(예를 들어, 본 발명의 위치 1은 PS51375의 위치 3에 해당함). 다만, "ii"(-2)번의 아미노산의 경우는, PPR 모티프를 구성하는 아미노산의 말단(C 말단측)으로부터 두 번째 아미노산, 또는 다음 PPR 모티프의 첫 번째 아미노산에 대하여 두 개 N 말단측, 즉 -2번째의 아미노산으로 한다. 다음 PPR 모티프가 명확하게 동정되지 않는 경우, 다음 나선 구조의 첫 번째 아미노산에 대하여 두 개 앞의 아미노산만을 "ii"로 한다. Pfam에 대해서는 http://pfam.sanger.ac.uk/, 그리고 Prosite에 대해서는 http://www.expasy.org/prosite/를 참조할 수 있다.
PPR 모티프의 보존된 아미노산 서열은 아미노산 수준에서는 낮은 보존성을 나타내지만, 2차 구조상에서의 두 개의 a-나선은 잘 보존되어 있다. 전형적인 PPR 모티프는 35개의 아미노산으로 구성되지만, 그것의 길이는 30 내지 38개의 아미노산으로 가변적이다.
보다 구체적으로, 본 발명에 사용된 용어 PPR 모티프는 식 1로 표시되는 30 내지 38개의 아미노산 길이의 폴리펩티드로 이루어진다:
식에서,
Helix A는 12개의 아미노산 길이의 a-나선 구조를 형성할 수 있는 모이어티이고, 식 2로 표시되며:
식 2에서, A1 내지 A12는 각각 독립적으로 아미노산을 나타내고;
X는 존재하지 않거나, 또는 1 내지 9개의 아미노산 길이로 이루어지는 모이어티이고;
Helix B는 11 내지 13개의 아미노산 길이로 이루어지는 a-나선 구조를 형성할 수 있는 모이어티이고;
L은 2 내지 7개의 아미노산 길이의 식 3으로 표시되는 모이어티이고:
식 3에서, 각 아미노산은 "i"(-1), "ii"(-2)로 C 말단측으로부터 넘버링되며,
다만, Liii 내지 Lvii은 존재하지 않을 수 있다.
달리 명시되지 않는 한, 본 발명에 사용된 용어 "PPR 단백질"은 상기 기술된 PPR 모티프를 1개 이상, 바람직하게는 2개 이상 가지는 PPR 단백질을 말한다. 달리 명시되지 않는 한, 본 설명에 사용된 용어 "단백질"은 폴리펩티드(복수의 아미노산이 펩티드 결합된 사슬)로 이루어지는 물질 전반을 말하며, 비교적 저분자의 폴리펩티드로 이루어지는 것들도 포함한다. 본 발명에 사용된 용어 "아미노산"은 통상적인 아미노산 분자를 나타낼 수 있고, 그렇지 않으면 경우에 따라 펩티드 사슬을 구성하는 아미노산 잔기를 나타낼 수 있다. 어느 것을 나타내고 있는지는 문맥으로부터 당업자에게 명백하다.
달리 명시되지 않는 한, PPR 모티프의 RNA 염기와의 결합성에 관하여 본 발명에 사용된 용어 "선택적"은 RNA 염기 중 어느 하나의 염기에 대한 결합 활성이 다른 염기에 대한 결합 활성보다 높은 것을 말한다. 당업자라면 이 선택성을 위한 실험을 계획하고 확인할 수 있으며, 당업자가 계산을 통해 결정할 수도 있다.
달리 명시되지 않는 한, 본 발명에 사용된 용어 "RNA 염기"는 RNA를 구성하는 리보뉴클레오티드의 염기를 나타내고, 구체적으로는 아데닌(A), 구아닌(G), 시토신(C) 또는 우라실(U) 중 어느 하나를 나타낸다. 또한, PPR 단백질은 RNA 내의 염기에 대하여 선택성을 가질 수 있지만, 핵산 단량체에 결합하지는 않는다는 점에 유의해야 한다.
PPR 단백질은 식물에 많이 존재하며, 애기장대(Arabidopsis thaliana)에서는 500개의 단백질, 약 5000개의 모티프가 발견될 수 있다. 벼, 포플러 및 부처손(Selaginella tamariscina)등의 여러 육상 식물에도 다양한 아미노산 서열을 갖는 PPR 모티프 및 PPR 단백질이 존재한다. 본 발명에서는 자연계에 존재하는 PPR 모티프 및 PPR 단백질을 사용할 수 있고, 예를 들어 WO2013/058404에 개시된 방법에 기초하여 설계된 PPR 모티프 및 PPR 단백질을 사용할 수도 있다. 구체적으로, 소정의 PPR 모티프 및 PPR 단백질은 WO2013/058404에 개시된 다음 정보에 기초하여 설계될 수 있다.
(I) 선택적 결합을 위해 중요한 아미노산의 위치에 관한 정보
PPR 모티프의 1, 4, "ii"(-1)번의 세 개의 아미노산의 조합(A1, A4, Lii), 또는 4, "ii"(-1)번의 두 개의 아미노산의 조합(A4, Lii)이 RNA 염기와의 선택적 결합을 위해 중요하며, 이들 조합에 의해 결합하는 RNA 염기가 어느 것인지를 결정할 수 있다.
본 발명은 WO2013/058404에 개시된 A1, A4 및 Lii의 세 개의 아미노산 조합 및/또는 A4 및 Lii의 두 개의 아미노산 조합에 대한 결과를 이용할 수 있다.
(II) A1, A4 및
Lii의
세 개의 아미노산 조합과 RNA 염기와의 대응에 대한 정보
(3-1) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 발린, 아스파라긴 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 C에, 그 다음으로 A 또는 G에 대하여 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-2) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 발린, 트레오닌 및 아스파라긴인 경우, 그 PPR 모티프는 A에 강하게 결합하고, 다음으로 G에, 그 다음으로 C에 대하여 결합하지만 U에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-3) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 발린, 아스파라긴 및 아스파라긴인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 A 또는 U에 대하여 결합하지만 G에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-4) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 글루탐산, 글리신 및 아스파르트산인 경우, 그 PPR 모티프는 G에 강하게 결합하지만 A, U 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-5) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 이소류신, 아스파라긴 및 아스파라긴인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 U에, 그 다음으로 A에 대하여 결합하지만 G에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-6) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 발린, 트레오닌 및 아스파르트산인 경우, 그 PPR 모티프는 G에 강하게 결합하고, 다음으로 U에 대하여 결합하지만 A와 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-7) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 리신, 트레오닌 및 아스파르트산인 경우, 그 PPR 모티프는 G에 강하게 결합하고, 다음으로 A에 대하여 결합하지만 U 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-8) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 페닐알라닌, 세린 및 아스파라긴인 경우, 그 PPR 모티프는 A에는 강하게 결합하고, 다음으로 C에, 그 다음으로 G 및 U에 대하여 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-9) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 발린, 아스파라긴 및 세린인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 U에 대하여 결합하지만 A 및 G에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-10) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 페닐알라닌, 트레오닌 및 아스파라긴인 경우, 그 PPR 모티프는 A에 강하게 결합하지만 G, U 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-11) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 이소류신, 아스파라긴, 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 A에 대하여 결합하지만 G 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-12) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 트레오닌, 트레오닌 및 아스파라긴인 경우, 그 PPR 모티프는 A에 강하게 결합하지만 G, U 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-13) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 이소류신, 메티오닌 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 C에 대하여 결합하지만 A 및 G에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-14) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 페닐알라닌, 프롤린 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 C에 대하여 결합하지만 A 및 G에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-15) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 티로신, 프롤린 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하지만 A, G 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(3-16) A1, A4 및 Lii의 세 개의 아미노산 조합이 순서대로 류신, 트레오닌 및 아스파르트산인 경우, 그 PPR 모티프는 G에 강하게 결합하지만 A, U 및 C에는 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(II) A4 및
Lii의
두 개의 아미노산 조합과 RNA 염기와의 대응에 대한 정보
(2-1) A4 및 Lii가 순서대로 아스파라긴 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 C, 그 다음으로 A 및 G에 대하여 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-2) A4 및 Lii가 순서대로 아스파라긴 및 아스파라긴인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 U, 그 다음으로 A 및 G에 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-3) A4 및 Lii가 순서대로 트레오닌 및 아스파라긴인 경우, 그 PPR 모티프는 A에 강하게 결합하고, 다음으로 G, U 및 C에 대하여 약하게 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-4) A4 및 Lii가 순서대로 트레오닌 및 아스파르트산인 경우, 그 PPR 모티프는 G에 대하여 강하게 결합하고, 다음으로 A, U 및 C에 대하여 약하게 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-5) A4 및 Lii가 순서대로 세린 및 아스파라긴인 경우, 그 PPR 모티프는 A에 강하게 결합하고, 다음으로 G, U 및 C에 대하여 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-6) A4 및 Lii가 순서대로 글리신 및 아스파르트산인 경우, 그 PPR 모티프는 G에 강하게 결합하고, 다음으로 U, 그 다음으로 A와 결합하지만 C에 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-7) A4 및 Lii가 순서대로 아스파라긴 및 세린인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 U, 그 다음으로 A 및 G에 대하여 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-8) A4 및 Lii가 순서대로 프롤린 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 G, C 및 C에 대하여 결합하지만 A에 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-9) A4 및 Lii가 순서대로 글리신 및 아스파라긴인 경우, PPR 모티프는 A에 강하게 결합하고, 다음으로 G에 대하여 결합하지만 C 및 U에 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-10) A4 및 Lii가 순서대로 메티오닌 및 아스파르트산인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 A, G 및 C에 대하여 약하게 결합하는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-11) A4 및 Lii가 순서대로 류신 및 아스파르트산인 경우, 그 PPR 모티프는 C에 강하게 결합하고, 다음으로 U에 대하여 결합하지만 A 및 G에 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
(2-12) A4 및 Lii가 순서대로 발린 및 트레오닌인 경우, 그 PPR 모티프는 U에 강하게 결합하고, 다음으로 A에 대하여 결합하지만 G 및 C에 결합하지 않는, 선택적인 RNA 염기 결합 능력을 갖는다.
[PPR 모티프 및 PPR 단백질의 이용]
동정 및 설계:
하나의 PPR 모티프는 RNA의 특정 염기를 인식할 수 있다. 그리고 본 발명에 따르면, 특정 위치의 아미노산을 적절히 배치함으로써 A, U, G, C 각각에 선택적인 PPR 모티프를 선택하거나 설계할 수 있다. 또한, 이러한 PPR 모티프의 적절한 연속을 함유하는 단백질은 그것의 상응하는 특이적인 서열을 인식할 수 있다. 또한, 상술한 결과에 의해, 원하는 RNA 염기에 선택적으로 결합할 수 있는 PPR 모티프 및 원하는 RNA에 서열 특이적으로 결합할 수 있는 복수 개의 PPR 모티프를 갖는 단백질을 설계할 수 있다. 설계할 때, PPR 모티프 내의 중요한 위치의 아미노산 이외의 모이어티는 천연형의 PPR 모티프의 서열 정보를 참고할 수 있다. 또한, 전체로서 천연형을 사용하여 상기의 중요한 위치의 아미노산만을 치환함으로써 설계할 수도 있다. PPR 모티프의 반복 수는 표적 서열에 따라 적절하게 결정될 수 있으나, 예를 들어 반복 수는 2개 이상, 또는 2 내지 30개일 수 있다.
상기와 같이 설계된 PPR 모티프 또는 PPR 단백질은 당업자에게 잘 알려져 있는 방법에 의해 제조할 수 있다. 예를 들어, 설계된 PPR 모티프 또는 PPR 단백질의 아미노산 서열로부터 이를 암호화하는 핵산 서열을 결정하고, 클로닝하여 원하는 PPR 모티프 또는 PPR 단백질을 생산하는 형질전환체(발현 벡터 등)를 제조할 수 있다.
융합 단백질의 제조 및 이용:
본 발명은 상기 기술된 PPR 모티프 또는 PPR 단백질(즉, 표적 mRNA에 대하여 RNA 염기 선택적으로 또는 RNA 염기서열 특이적으로 결합할 수 있는 폴리펩티드)과 mRNA로부터의 단백질 발현량을 향상시키는 1개 이상의 기능적 도메인과의 융합 단백질에 관한 것이다.
본 발명에서 사용될 수 있는 "mRNA로부터의 단백질 발현량을 향상시키는 기능적 도메인"은 예를 들어, mRNA의 번역을 직접적 또는 간접적으로 촉진하는 것이 알려져 있는 단백질의 기능적 도메인의 전부 또는 기능적인 일부일 수 있다. 보다 구체적으로, 본 발명에서 사용될 수 있는 기능적 도메인은 예를 들어, mRNA로 리보솜을 유도하는 도메인, mRNA의 번역개시 또는 번역촉진과 관련된 도메인, mRNA의 핵 외로의 수송과 관련된 도메인, 소포체 막에 대한 결합과 관련된 도메인, 소포체 보유 신호(ER 보유 신호) 서열을 함유하는 도메인, 또는 소포체 신호 서열을 함유하는 도메인일 수 있다.
보다 구체적으로, 상기 mRNA로 리보솜을 유도하는 도메인은 DENR(밀도 조절된 단백질), MCT-1(악성 T-세포 증폭된 서열 1), TPT1(번역 제어된 종양 단백질) 및 Lerepo4(징크 핑거 CCCH-도메인)로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인일 수 있다. 또한, 상기 mRNA의 번역개시 또는 번역촉진과 관련된 도메인은 eIF4E 및 eIF4G로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인일 수 있다. 또한, mRNA의 핵 외로의 수송과 관련된 도메인은 SLBP(스템-루프 결합 단백질)의 전부 또는 기능적인 일부를 함유하는 도메인일 수 있다. 또한, 소포체 막에 대한 결합과 관련된 도메인은 SEC61B, TRAP-알파(트랜스로콘 관련 단백질 알파), SR-알파, Dia1(시토크롬 b5 환원효소 3) 및 p180으로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인일 수 있다. 또한, 상기 소포체 보유 신호(ER 보유 신호) 서열은 KDEL(KEEL) 서열을 함유하는 신호 서열일 수 있다. 또한, 상기 소포체 신호 서열은 MGWSCIILFLVATATGAHS(서열번호 22)를 함유하는 신호 서열일 수 있다.
본 발명에 따른 융합 단백질에서, 기능적 도메인은 PPR 단백질의 N 말단측에 융합될 수 있거나, C 말단측에 융합될 수 있거나, 이의 N 말단측과 C 말단측 양쪽 모두에 융합될 수 있다. 또한, 본 발명에 따른 융합 단백질은 여러 개의 기능적 도메인(예를 들어, 2 내지 5개의 기능적 도메인)을 포함할 수 있다. 또한, 본 발명에 따른 융합 단백질에서, 기능적 도메인과 PPR 단백질은 예를 들어, 링커를 통해 간접적으로 융합될 수 있다.
본 발명은 상기 기술된 융합 단백질을 암호화하는 핵산 및 이 핵산을 포함하는 벡터(예를 들어, 발현 벡터)에 관한 것이다. 본 발명에서, 발현 벡터는 예를 들어, 상류로부터 프로모터 서열을 갖는 DNA, 원하는 단백질을 암호화하는 DNA 및 터미네이터 서열을 갖는 DNA를 의미하지만, 원하는 기능을 나타내는 반드시 이 순서대로 배열될 필요는 없다. 본 발명에서는 당업자가 통상적으로 사용할 수 있는 여러 가지 발현 벡터를 사용할 수 있다.
본 발명에 따른 융합 단백질은 진핵생물의 RNA 번역 기구를 이용하기 때문에, 진핵생물(예를 들어, 동물, 식물, 미생물(예컨대, 효모) 및 원생생물)의 세포에서 기능 할 수 있다. 본 발명에 따른 융합 단백질은 특히, 동물 세포 내(시험관 내(in vitro) 또는 생체 내(in vivo)에서)에서 기능 할 수 있다. 본 발명에 따른 융합 단백질 또는 본 발명에 따른 융합 단백질을 발현하는 벡터가 도입될 수 있는 동물 세포의 예로는 인간, 원숭이, 돼지, 소, 말, 개, 고양이, 마우스 및 랫트 유래의 세포를 들 수 있다. 또한, 본 발명에 따른 융합 단백질 또는 본 발명에 따른 융합 단백질을 발현하는 벡터가 도입될 수 있는 배양 세포의 예로는 중국 햄스터 난소(CHO) 세포, COS-1 세포, COS-7 세포, VERO(ATCC CCL-81) 세포, BHK 세포, 개 신장 유래 MDCK 세포, 햄스터 AV-12-664 세포, HeLa 세포, WI38 세포, 293 세포, 293T 세포 및 PER.C6 세포를 들 수 있으나, 이에 한정되지 않는다.
본원에서 사용되는 용어는 특별히 정의된 것을 제외하고 특정 구현예를 설명하기 위하여 사용된 것으로, 본 발명을 한정하고자 하는 것이 아니다.
또한, 본원에서 사용된 용어 "포함하다"는 문맥상 명백히 다른 이해를 필요로 하지 않는 한, 기술된 사항(예컨대, 부재, 단계, 구성요소, 숫자 등)이 존재함을 의도하고자 하는 것으로, 그 이외의 사항(예컨대, 부재, 단계, 구성요소, 숫자 등)의 존재를 배제하고자 하는 것은 아니다.
달리 정의되지 않는 한, 본원에서 사용되는 모든 용어(기술 용어 및 과학 용어를 포함)는 본 발명이 속하는 분야의 당업자가 광범위하게 이해하는 바와 동일한 의미를 갖는다. 달리 명확하게 정의되지 않는 한, 본원에서 사용되는 용어는 본 명세서 및 관련 기술 분야에서의 의미와 일관된 의미를 갖는 것으로 해석되어야 하며, 이상화된 또는 과도하게 형식적인 의미로 해석되어서는 안 된다.
도 1은 실시예에서 사용된 이펙터 플라스미드와 리포터 플라스미드의 모식도 및 실험 개요의 모식도를 나타낸다. 도 1A는 실시예에서 사용된 이펙터 플라스미드와 리포터 플라스미드의 모식도를 나타낸다. 이펙터 플라스미드로부터는 PPR 모티프와 eIF4G의 융합 단백질이 발현된다. 본 실시예에서는 표적 서열에 관하여 잘 연구되어 있는 CRR4 단백질을 사용하였다. 리포터 플라스미드로부터는 레닐라 루시페라아제(RLuc) 및 반딧불이 루시페라아제(FLuc)가 디시스트론 mRNA의 형태로 전사된다. PPR 결합 서열(여기서, CRR4 결합 서열)을 FLuc의 5' 측에 삽입하였다. 도 1B는 본 실시예의 실험개요의 모식도를 나타낸다. PPR 결합 서열의 유무와 관계없이, RLuc는 유사한 수준으로 번역된다. 이러한 이유로 RLuc의 활성값은 이 리포터 시스템에서의 형질감염의 대조군으로서 처리될 수 있다. Fluc의 번역은 PPR-eIF4G가 PPR 결합 서열에 결합하여, eIF4G의 효과에 의해 번역 인자를 유인할 수 있을 때에만 개시된다. 한편, PPR 결합 서열이 존재하지 않고 PPR-eIF4G가 결합할 수 없는 경우, FLuc의 번역은 낮은 수준으로 유지된다.
도 2는 HEK293T 세포를 이용한 리포터 분석법의 실험 절차를 나타낸다.
도 3은 실시예 1의 실험 결과를 나타낸다. 서열 특이적 번역의 활성화는 CRR4-eIF4G와 PPR 결합 서열에 의존한다. 이 실험은 CRR4-Flag(번역 활성화 인자 없음, 흰색) 또는 CRR4-eIF4G(번역 활성화 인자 있음, 회색)가 삽입된 이펙터 플라스미드, 및 PPR 결합 서열을 삽입 또는 삽입하지 않은 리포터 벡터를 사용하여 수행하였다. 결과로부터, PPR-eIF4G와 PPR 결합 서열 모두의 존재하에서 특이적으로 2.75배의 번역 활성이 확인되었다. 값은 평균과 표준 편차를 나타낸다(N = 3).
도 4는 실시예 2의 실험의 개요를 나타낸다.
도 5은 실시예 2의 실험 결과 및 도메인의 기능의 설명을 나타낸다.
도 6은 실시예 2의 실험 결과 및 도메인의 기능의 설명을 나타낸다.
도 2는 HEK293T 세포를 이용한 리포터 분석법의 실험 절차를 나타낸다.
도 3은 실시예 1의 실험 결과를 나타낸다. 서열 특이적 번역의 활성화는 CRR4-eIF4G와 PPR 결합 서열에 의존한다. 이 실험은 CRR4-Flag(번역 활성화 인자 없음, 흰색) 또는 CRR4-eIF4G(번역 활성화 인자 있음, 회색)가 삽입된 이펙터 플라스미드, 및 PPR 결합 서열을 삽입 또는 삽입하지 않은 리포터 벡터를 사용하여 수행하였다. 결과로부터, PPR-eIF4G와 PPR 결합 서열 모두의 존재하에서 특이적으로 2.75배의 번역 활성이 확인되었다. 값은 평균과 표준 편차를 나타낸다(N = 3).
도 4는 실시예 2의 실험의 개요를 나타낸다.
도 5은 실시예 2의 실험 결과 및 도메인의 기능의 설명을 나타낸다.
도 6은 실시예 2의 실험 결과 및 도메인의 기능의 설명을 나타낸다.
이하, 본 발명을 실시예를 참조하여 더욱 상세하게 설명한다. 그러나 본 발명은 다양한 양태로 구현될 수 있으며, 아래 기술된 실시예에 한정되는 것으로 해석되어서는 안 된다.
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실시예
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실시예 1: PPR 모티프와 eIF4G의 융합 단백질에 의한 표적 mRNA로부터의 단백질 발현량의 향상
재료
(장치)
- 분자생물학 실험을 위한 기본 설비(플라스미드 구축을 위한 것 등)
- 도립현미경(DM IL S40, Leica Microsystems, 독일 베츨라어 소재)
- CO2 인큐베이터(KM-CC17RH2, Panasonic Healthcare, 일본 도쿄 소재)
- 클린 벤치(MHE-S1300A2, Panasonic Healthcare, 일본 도쿄 소재)
- 흡인기(SP-30, Air Liquide Medical Systems, 이탈리아 보베초 BS 소재)
- 원심분리기(스윙 로터) (LC-200, Tomy Seiko, 일본 도쿄 소재)
- 초저온 냉동고(-80℃)(MDF-C8V, Panasonic Healthcare, 일본 도쿄 소재)
- 플레이트 판독기(EnSight Kaleido, PerkinElmer, 미국 매사추세츠 주 월섬 소재)
(세포 배양)
- HEK293T 세포주(주석 1 참조)
- 둘베코 변형 이글 배지(DMEM, 고 글루코오스)(주석 2 참조)
- 100× 페니실린-스트렙토마이신 용액
- 우태아혈청(FBS)(주석 3 참조)
- EDTA-NaCl 용액: 10 mM EDTA 및 0.85% (w/v) NaCl, pH를 7.2 내지 7.4로 조정, 오토클레이브 멸균, 실온 저장
- 100 × 20 mm 세포 배양 페트리 접시(Greiner bio one, 독일 프리켄하우젠 소재)
- 10 mL 일회용 멸균 피펫
- 15 mL 및 50 mL 플라스틱 원심분리 튜브
- 1.8 mL 동결튜브(Nunc; Thermo Fisher Scientific, 미국 매사추세츠 주 월섬 소재)
- 동결 컨테이너(Nalgene; Thermo Fisher Scientific, 미국 매사추세츠 주 월섬 소재)
- Bambanker(Lymphotec, 일본 도쿄 소재)
(형질감염)
- 이펙터 플라스미드: pcDNA3.1(Thermo Fisher Scientific, 미국 매사추세츠 주 월섬 소재)을 기본 벡터로 사용하였다. PPR과 eIF4G의 융합 유전자를 발현 카세트 내로 삽입하였다(100 ng/μL)(주석 4 참조).
- 리포터 플라스미드: pcDNA3.1(Thermo Fisher Scientific, 미국 매사추세츠 주 월섬 소재)을 기본 벡터로 사용하였다. 루시페라아제 유전자를 발현 카세트 내로 삽입하고, PPR 결합 서열을 그것의 5'-UTR 내로 삽입하였다(100 ng/μL).
- 폴리-L-리신 코팅된 96-웰 플레이트(AGC Techno glass, 일본 시즈오카 소재)
- 1× 인산염 완충 식염수, PBS(-): 1.47 mM KH2PO4, 8.1 mM Na2HPO4, 137 mM NaCl, 및 2.7 mM KCl. pH를 7.4로 조정, 오토클레이브 멸균, 실온 저장
- (세포 계수를 위한) 혈구 계산기(Improved Neubauer Type Cell counter plate, Watson, 일본 효고 소재)
- 형질감염 시약(HilyMax, Dojindo Molecular Technologies, 일본 쿠마모토 소재)
(루시페라아제 분석법)
- 듀얼-글로 루시페라아제 분석 시스템(Dual-Glo Luciferase Assay System, Promega, 미국 위스콘신 주 매디슨 소재)
- 96-웰 광도계 플레이트(96-well luminometer plate, PerkinElmer, 미국 매사추세츠 주 월섬 소재).
실험 방법
(벡터의 구축)
리포터 분석법에는 이펙터 플라스미드 및 리포터 플라스미드가 필요하며, 이 두 가지 플라스미드 모두 pcDNA3.1을 기반으로 하여 구축하였다. 이펙터 플라스미드는 PPR 단백질 및 인간 eIF4G의 부분적 도메인(서열번호 1)을 암호화하는 융합 단백질을 포함한다(도 1A). PPR 단백질 모이어티는 CRR4(서열번호 2)를 사용하였다. 리포터 플라스미드 측에는 레닐라 루시페라아제(RLuc)와 반딧불이 루시페라아제(FLuc)의 두 개의 오픈 리딩 프레임(ORF)을 포함하고 있으며, 이들은 디시스트론으로 전사된다(도 1A). RLuc 유전자는 FLuc 유전자의 5'-말단 측에 위치하고 있으며, 유전자 발현의 대조군으로 사용하였다. PPR 결합 영역은 FLuc의 ORF의 5'-UTR 로 삽입되며, 4-염기서열(ATCG 및 GATC)에 의해 중단되는 CRR4 인식서열(5'-UAUCUUGUCUUUA-3')(서열번호 3)의 3회의 반복으로 이루어진다. 융합된 이펙터 유전자 및 리포터 유전자 둘 모두를 발현시키기 위하여, 거대세포 바이러스 프로모터(CMV) 및 소 성장 호르몬 유전자 유래 폴리아데닐화 신호를 사용하였다. 대조군 실험을 위해, eIF4G를 갖지 않는 이펙터 플라스미드를 PPR에 FLAG 에피토프 태그를 융합시킴으로써 구축하였다. 또한, PPR 결합 영역을 갖지 않는 대조군 리포터 플라스미드도 구축하였다.
실시예의 세포 배양에서 리포터 분석법까지의 절차 개요를 도 2에 묘사하였다.
(동결 스톡으로부터의 세포 배양)
본 공정은 무균적으로 실시하였다. 모든 도구는 70% 에탄올로 미리 소독하였다.
1. 9 mL DMEM 배양 배지를 15 mL 원심분리 튜브(살균됨)에 넣는다.
2. 동결튜브 안의 1 mL의 HEK293T 동결세포를 37℃의 수조에서 배양하여 신속하게 융해시킨다.
3. 이 세포를 9 mL DMEM을 함유하는 15 mL 원심분리 튜브에 넣는다.
4. 실온에서 1100 x g, 2분간 원심분리하고, 상청액을 제거한다.
5. 이 세포를 10 mL DMEM(최종 농도가 10%가 되도록 FBS를 첨가)에 재현탁시킨다.
6. 재현탁된 세포를 100 mm 페트리 접시로 옮긴다. 페트리 접시를 37℃, 5% CO2 조건하의 인큐베이터에 정치한다. 동결 스톡으로부터 배양을 시작한 경우, 배양세포는 24시간 후에 계대한다.
건강한 세포 상태를 유지하기 위해(주석 5 참조), 페트리 접시 표면에서의 세포 밀도를 10% 내지 80%로 유지한다. 계대는 기본적으로 3일마다(주 2회) 수행하거나, 세포의 성장률에 따라 수행한다. 또한, 계대 횟수를 적게 유지하기 위하여, 세포는 월 1회 동결 스톡으로부터 새롭게 배양한다. 계대 횟수를 적게 유지하여 세포의 건강한 상태를 유지하는 것이 효율적인 DNA 형질감염에 중요하다.
(세포 유지를 위한 계대)
1. 새로운 100 mm 페트리 접시를 필요한 만큼 준비한다. 8 mL의 DMEM과 1 mL의 FBS를 각각의 페트리 접시에 미리 첨가한다.
2. 배양세포를 함유하는 페트리 접시 상의 배지를 흡인기로 제거한다(주석 6 참조).
3. 2 mL EDTA-NaCl 용액을 페트리 접시 내 표면의 부착 세포 위에 세포가 떨어져 나가지 않도록 살살 첨가한다. 페트리 접시를 회전시켜 용액이 페트리 접시의 전체 표면에 걸쳐 고르게 분포되도록 한다. EDTA-NaCl 용액을 흡인기로 제거한다다. 페트리 접시를 가볍게 두드려 세포를 떼어낸다.
4. 10 mL DMEM을 페트리 접시의 세포에 첨가하고, 부드럽게 피펫팅하여 세포를 현탁시킨다.
5. 미리 준비하여 각각 9 mL 배양 배지를 함유하는 페트리 접시에 1 mL의 현탁된 세포(10% 배양 세포)를 첨가한다. 페트리 접시 각각을 회전시켜 그것의 전체 표면에 걸쳐 세포가 분포되도록 한다.
(세포의 동결 보관)
Bambanker 시약 및 대수증식 중의 최대 50%의 세포 밀도의 배양세포를 사용하여 동결 스톡을 제조한다. Bambanker의 사용에 의해 높은 회수율과 장기적인 보관이 용이해진다.
1. 계대 후 이틀째의 세포를 계대시의 절차에 따라 떼어낸다. 5 내지 10 mL DMEM을 첨가하고, 세포를 50 mL 원심분리 튜브에 회수한다.
2. 실온에서, 1100 x g, 2분 동안 원심분리하고, 상청액을 제거한다.
3. 페트리 접시당 1 mL의 Bambanker를 첨가하여 세포를 현탁시킨다.
4. 현탁 세포를 신속하게 동결튜브로 분주하고, 뚜껑을 닫는다.
5. 전용 동결 컨테이너에 넣고, -80℃에서 12시간 동안 정치한다(주석 7 참조).
6. 표준 샘플 박스로 옮기고, -80℃ 또는 액체 질소에 저장한다.
(일시적인 유전자 도입(형질감염))
1. 형질감염을 개시하기 전에, 계대 후 이틀째의 세포를 함유하는 페트리 접시를 필요한 만큼 준비하고, 세포가 건강한지(정상) 여부를 확인한다(주석 8 참조). 대략 어림잡아 하나의 페트리 접시에서 96회 분석을 수행할 수 있다.
2. 계대 후 이틀째의 세포를 계대시의 절차에 따라 떼어내고, 재현탁시킨 세포를 50 mL 원심분리 튜브로 옮긴다.
3. 실온에서, 1100 x g, 2분 동안 원심분리하고, 상청액을 제거한다.
4. 세포괴를 10 mL DMEM(최종 농도가 10%가 되도록 FBS를 첨가)에 완전히 분산시킨다.
5. 혈구 계산기와 도립 현미경을 사용하여 세포를 계수한다. 세포 수가 1 내지 2 × 105개 세포/mL이 되도록, 적당량의 DMEM(최종 농도가 10%가 되도록 FBS를 첨가)에 현탁시킨다.
6. 96-웰 플레이트를 준비한다. 각 웰당 200 μL(2 내지 4 × 104개 세포/mL)의 현탁 배양 세포를 넣고, 플레이트를 5% CO2 조건하의 37℃의 인큐베이터에 밤새 정치한다. 1회 분석에 한 개의 웰이 사용된다.
7. 다음날, 각 웰로부터 배지를 조심스럽게 제거하고, 100 μL의 새로운 DMEM(최종 농도가 10%가 되도록 FBS를 첨가)으로 교체한다.
8. 400 ng의 이펙터 플라스미드(100 ng/μL을 4 μL) 및 100 ng의 리포터 플라스미드(100 ng/μL을 1 μL)를 새로운 96-웰 PCR 플레이트(또는 0.2 mL 튜브) 상의 단일 웰에 넣는다.
9. 1회 분석 당, 1 μL의 HilyMAX를 10 μL의 무혈청 DMEM으로 희석한다.
10. 11 μL 희석 용액을 플라스미드를 함유하는 모든 웰에 넣는다. 피펫팅하여 용액을 잘 혼합한다.
11. 실온에서 15분간 정치한다. 혼합물 전량을 배양 세포를 함유하는 웰에 넣는다. 37℃, 5% CO2 조건하의 인큐베이터에 24시간 정치한다.
(루시페라아제 분석법)
몇 가지 변경을 제외하고는 제조사의 사용 지침에 따라 듀얼-글로 루시페라아제 분석 시스템을 이용하여 이중 루시페라아제 분석을 수행한다.
1. 형질감염 24시간 후, 각 웰의 배지를 40 μL 1× PBS(-)로 교환한다.
2. 듀얼-글로 루시페라아제 시약 40 μL을 각 웰에 넣고, 피펫팅하여 배양 배지와 잘 혼합한다.
3. 실온에서 10분간 정치하고, 전량을 96-웰 광도계 플레이트로 옮긴다.
4. FLuc 유전자 발현과 관련된 반딧불이 루시페라아제에 의한 발광을 플레이트 판독기로 측정한다.
5. 듀얼-글로 스톱 & 글로 완충액으로 스톱 & 글로(Stop & Glo) 기질을 100배 희석한다. 희석된 용액 40 μL을 각 웰에 첨가한다.
6. 적어도 실온에서 10분간 정치하고, 그로부터 RLuc 유전자 발현과 관련된 레닐라 루시페라아제에 의한 발광을 측정한다.
(데이터 분석)
1. 분석 간의 형질감염 효율의 차이나 실험 오차를 보정하기 위하여, FLuc/RLuc의 값을 계산한다.
2. 리포터 유전자 발현 활성의 증가를 PPR 결합 영역의 존재 및 이의 부재 하에 각각에 대하여, 본 발명에 따른 플라스미드(CRR4와 번역 활성화 도메인 eIF4G와의 융합 단백질을 암호화하는 플라스미드)를 이용하여 얻어진 실험값을 대조군 플라스미드(CRR4와 FLAG-태그와의 융합 단백질을 암호화하는 플라스미드)를 이용하여 얻어진 실험값으로 나눔으로써 구한다.
실험 결과
루시페라아제 분석법 결과를 도 3에 나타내었다. 도 3에 나타낸 바와 같이, PPR-eIF4G와 PPR 결합 서열 모두의 존재하에서 특이적으로 2.75배 번역 활성이 확인되었다. 즉, PPR 단백질과 mRNA로부터의 단백질 발현량을 향상시키는 기능적 도메인과의 융합 단백질은 표적 mRNA로부터의 단백질 발현량을 향상시킨다는 것을 보여준다.
주석
(주석 1) HEK293T는 SV40 큰 T 항원을 발현하는 인간 태아 유래 신장 세포주이다. 이 세포주는 배양이 용이하고, 다양한 방법에 의해 고효율로 형질감염될 수 있다. HEK293T 세포는 RIKEN BRC(ja.brc.riken.jp) 또는 ATCC(www.atcc.org)로부터 입수 가능하다.
(주석 2) DMEM은 미생물 오염을 방지하기 위하여 1× 페니실린-스트렙토마이신 용액이 첨가된다.
(주석 3) 사용 전, FBS는 30분 동안 56℃에서 불활성화되어, 4℃에 저장된다.
(주석 4) 플라스미드의 순도는 형질감염 효율에 매우 중요하다. 플라스미드는 형질감염 등급의 키트를 이용하여 단리되어야 한다.
(주석 5) 일간 성장률은 세포가 건강함을 나타내는 지표이다. 세포 성장이 억제되는 것을 막기 위하여, 세포는 항상 충분한 공간과 영양 조건하에서 배양되어야 한다.
(주석 6) HEK293T 세포는 배양 페트리 접시로부터 용이하게 떨어져 나가므로, 배지를 교환할 때 살살 취급하여야 한다.
(주석 7) 전용 동결 컨테이너는 동결 속도를 조정할 수 있는 상자이고(-80 ℃에서 분당 약 -1℃), 그리고 이것에 의해 비프로그래밍 식의 -80℃ 냉동고에서의 동결 저장이 가능하다.
(주석 8) 형질감염에 관하여, 50 내지 80%의 배양 밀도에서의 세포를 사용한다. 그러나 적당한 세포 밀도는 형질감염 시약에 의존한다. 추가적으로, 플라스미드 DNA(μg)에 대한 형질감염 시약(μL)의 비율 또한 제조사의 사용 설명서에 따라 최적화되어야 한다. 본원에 기술된 절차는 96-웰 플레이트에서, HEK293T 세포, 형질감염 시약으로서 HilyMAX를 사용한 조건에 최적화된 것이다.
실시예 2: PPR과 다른 기능적 도메인과의 융합 단백질에 의한 표적 mRNA로부터의 단백질 발현량의 향상
세포를 이용하여 유용한 물질을 생산하는 경우, 내인성 유전자 및 외인성 유전자의 단백질 합성량을 정밀하게 제어할 필요가 있다. 최종 단백질 합성량은 유전자의 삽입 위치, mRNA 전사량, 전사 후 억제(RNA 수준에서의 억제), 번역 후 변형 등에 의해 결정된다. 이러한 이유로, PPR 단백질 서열이 표적 RNA 분자와 서열 특이적으로 결합한다는 사실을 이용한, mRNA의 번역을 증진시키는 방법을 고안하였다(도 4). 진핵생물에서 mRNA 번역은 번역 개시 인자(진핵 개시 인자(eukaryotic initiation factor; elF)가 mRNA에 개재되고, 그 결과 리보솜이 번역 개시점 근처로 동원됨으로써 개시된다. 즉, mRNA 상으로 리보솜을 모을 수 있다면 번역의 인위적인 증강이 가능하다고 생각하였다. 또한, mRNA의 단백질로의 번역은 일반적으로 ER에서 수행된다. 이러한 이유로, ER로 표적 mRNA를 적극적으로 국재화시킴으로써 번역을 증강시킬 수 있다고 생각하였다.
검증 실험
상기의 아이디어를 검증하기 위하여, 동물 배양 세포(HEK293T)를 이용하는 리포터 분석 시스템을 준비하였다(상이한 기능적 도메인이 사용되었다는 점을 제외하고, 실시예 1에 기재된 방법과 동일한 방법으로 실험을 수행함). 특정 RNA 서열(UAUCUUGUCUUUA)(서열번호 3)에 결합한다는 것이 알려져 있는 CRR4 단백질(애기장대 PPR 단백질 중 하나)을 이용하여 시스템을 구축하였다. 먼저, CRR4와 후보 단백질 기능적 도메인과의 융합 단백질 발현 벡터(이펙터 플라스미드)를 제조하였다. 후보 도메인은 (a) eIF 단백질(eIF4E 및 eIF4G), (b) 리보솜 결합 단백질(DENR, MCT-1, TPT1 및 Lerepo4), (c) 전사된 mRNA의 핵에서 세포질로의 수송을 촉진하는 히스톤의 번역 억제 인자(SLBP), (d) ER 앵커 단백질(SEC61B, TRAP-알파, SR-알파, Dia1 및 p180), (e) ER 보유 신호(KDEL) 및 (f) ER 신호 펩티드를 선택하였다. HA-CRR4-XX 또는 XX-CRR4-HA의 형태로 발현되도록 융합 단백질을 클로닝하였다(HA: 에피토프 태그(서열번호 4); XX: 후보 도메인).
리포터 플라스미드는 CMV 프로모터의 제어하에서 레닐라 루시페라아제(RLuc)와 반딧불이 루시페라아제(FLuc)가 디시스트론 mRNA의 형태로 전사되는 발현 카세트를 포함하였다. Fluc의 5' 말단측에 PPR 결합 서열(UAUCUUGUCUUUA)(서열번호 3)이 3개 삽입되어 있다.
이펙터 플라스미드와 리포터 플라스미드를 HEK293T 세포 내로 형질감염시키고, RLUC 및 FLUC의 발광량을 측정하였다. RLUC의 발광량을 형질감염 대조군으로 처리하였고, FLUC의 발광량/RLUC의 발광량의 값을 번역 활성량으로 처리하였다.
결과
다음 (A)와 (B)의 지표를 이용하여, 도 5와 도 6에 나타낸 결과를 검토하였다.
(A) 표적 부재하 및 존재하의 비교
서열 특이적으로 어느 정도 번역량 변화가 있었는지를 알 수 있다.
(B) 표적 존재하, 이펙터의 부재(empty)와 비교(검은색 파선)
도메인 추가에 따른 번역 변화량을 알 수 있다.
1. CRR4의 C 말단측에 eIF4E를 융합
(A) 2.7배
(B) 1.6배
2. CRR4의 C 말단측에 eIF4G를 융합
(A) 4.5배
(B) 3.3배
3. CRR4의 N 말단측에 DENR을 융합
(A) 1.7배
(B) 1.3배
4. CRR4의 C 말단측에 DENR을 융합.
(A) 2.4배
(B) 1.7배
5. CRR4의 N 말단측에 MCT-1을 융합
(A) 1.3배
(B) 1.0배
6. CRR4의 C 말단측에 MCT-1을 융합
(A) 2.0배
(B) 1.2배
7. CRR4의 N 말단측에 TPT-1을 융합
(A) 1.4배
(B) 1.0배
8. CRR4의 C 말단측에 TPT-1을 융합
(A) 2.4배
(B) 1.9배
9. CRR4의 N 말단측에 Lerepo4를 융합
(A) 3.0배
(B) 1.8배
10. CRR4의 C 말단측에 Lerepo4를 융합
(A) 3.3배
(B) 2.6배
11. CRR4의 C 말단측에 SLBP를 융합
(A) 4.1배
(B) 3.3배
12. CRR4의 C 말단측에 Sec61B를 융합
(A) 1.6배
(B) 1.6배
13. CRR4의 C 말단측에 Sec61BTM을 융합
(A) 2.4배
(B) 1.9배
14. CRR4의 C 말단측에 TRAP-알파를 융합
(A) 3.5배
(B) 4.5배
15. CRR4의 C 말단측에 TRAPTM을 융합
(A) 2.3배
(B) 1.6배
16. CRR4의 N 말단측에 SR-알파를 융합
(A) 1.7배
(B) 1.5배
17. CRR4의 N 말단측에 Dia1TM을 융합
(A) 1.8배
(B) 1.2배
18. CRR4의 N 말단측에 P180TM2R을 융합
(A) 2.1배
(B) 1.5배
19. CRR4의 N 말단측에 P180TMH를 융합
(A) 2.3배
(B) 2.5배
20. CRR4의 N 말단측에 P180TM2를 융합
(A) 3.0배
(B) 2.1배
21. CRR4의 C 말단측에 KDEL을 융합
(A) 1.8배
(B) 1.4배
22. CRR4의 C 말단측에 KEEL을 융합
(A) 2.3배
(B) 2.1배
23. CRR4의 N 말단측에 신호 펩티드(SP)를 융합
(A) 1.4배
(B) 2.0배
상기와 같이, 지표 (A) 및 표적 (B) 중 어느 것에 있어서도 모든 기능적 도메인에서 번역의 상승이 확인되었다. 즉, 본 발명에 따른 융합 단백질에 의해 표적 mRNA의 번역을 증강시킬 수 있음이 명백하게 밝혀졌다.
본 실시예에서 사용된 기능적 도메인의 아미노산 서열을 아래에 나타내었다:
SEQUENCE LISTING
<110> KYUSHU UNIVERSITY, NATIONAL UNIVERSITY CORPORATION
<120> Fusion Protein For Increasing Protein Expression From A Target
mRNA
<130> P18-208-INP-TACT
<150> US62/345252
<151> 2016-06-03
<150> JP2016-120524
<151> 2016-06-17
<160> 22
<170> PatentIn version 3.5
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Ser Phe Gly Met Trp Lys Asp Val Arg Arg Val Arg Thr Met Met Lys
515 520 525
Glu Arg Lys Ile Glu Lys Ile Pro Gly Cys Ser Trp Ile Glu Leu Asp
530 535 540
Gly Arg Val His Glu Phe Phe Val Asp Ser Ile Glu Val Ser Ser Thr
545 550 555 560
Leu
<210> 3
<211> 13
<212> RNA
<213> Artificial Sequence
<220>
<223> Synthetic RNA
<400> 3
uaucuugucu uua 13
<210> 4
<211> 12
<212> PRT
<213> Artificial Sequence
<220>
<223> Synthetic peptide
<400> 4
Met Ala Gly Tyr Pro Tyr Asp Val Pro Asp Tyr Ala
1 5 10
<210> 5
<211> 220
<212> PRT
<213> Homo sapiens
<400> 5
Met Ala Thr Val Glu Pro Glu Thr Thr Pro Thr Pro Asn Pro Pro Thr
1 5 10 15
Thr Glu Glu Glu Lys Thr Glu Ser Asn Gln Glu Val Ala Asn Pro Glu
20 25 30
His Tyr Ile Lys His Pro Leu Gln Asn Arg Trp Ala Leu Trp Phe Phe
35 40 45
Lys Asn Asp Lys Ser Lys Thr Trp Gln Ala Asn Leu Arg Leu Ile Ser
50 55 60
Lys Phe Asp Thr Val Glu Asp Phe Trp Ala Leu Tyr Asn His Ile Gln
65 70 75 80
Leu Ser Ser Asn Leu Met Pro Gly Cys Asp Tyr Ser Leu Phe Lys Asp
85 90 95
Gly Ile Glu Pro Met Leu Glu Asp Glu Lys Asn Lys Arg Gly Gly Arg
100 105 110
Trp Leu Ile Thr Leu Asn Lys Gln Gln Arg Arg Ser Asp Leu Asp Arg
115 120 125
Phe Trp Leu Glu Thr Leu Leu Cys Leu Ile Gly Glu Ser Phe Asp Asp
130 135 140
Tyr Ser Asp Asp Val Cys Gly Ala Val Val Asn Val Arg Ala Lys Gly
145 150 155 160
Asp Lys Ile Ala Ile Trp Thr Thr Glu Cys Glu Asn Arg Glu Ala Val
165 170 175
Thr His Ile Gly Arg Val Tyr Lys Glu Arg Leu Gly Leu Pro Pro Lys
180 185 190
Ile Val Ile Gly Tyr Gln Ser His Ala Asp Thr Ala Thr Lys Ser Gly
195 200 205
Ser Thr Thr Lys Asn Arg Phe Val Val Gly Arg Tyr
210 215 220
<210> 6
<211> 198
<212> PRT
<213> Homo sapiens
<400> 6
Met Ala Ala Asp Ile Ser Glu Ser Ser Gly Ala Asp Cys Lys Gly Asp
1 5 10 15
Pro Arg Asn Ser Ala Lys Leu Asp Ala Asp Tyr Pro Leu Arg Val Leu
20 25 30
Tyr Cys Gly Val Cys Ser Leu Pro Thr Glu Tyr Cys Glu Tyr Met Pro
35 40 45
Asp Val Ala Lys Cys Arg Gln Trp Leu Glu Lys Asn Phe Pro Asn Glu
50 55 60
Phe Ala Lys Leu Thr Val Glu Asn Ser Pro Lys Gln Glu Ala Gly Ile
65 70 75 80
Ser Glu Gly Gln Gly Thr Ala Gly Glu Glu Glu Glu Lys Lys Lys Gln
85 90 95
Lys Arg Gly Gly Arg Gly Gln Ile Lys Gln Lys Lys Lys Thr Val Pro
100 105 110
Gln Lys Val Thr Ile Ala Lys Ile Pro Arg Ala Lys Lys Lys Tyr Val
115 120 125
Thr Arg Val Cys Gly Leu Ala Thr Phe Glu Ile Asp Leu Lys Glu Ala
130 135 140
Gln Arg Phe Phe Ala Gln Lys Phe Ser Cys Gly Ala Ser Val Thr Gly
145 150 155 160
Glu Asp Glu Ile Ile Ile Gln Gly Asp Phe Thr Asp Asp Ile Ile Asp
165 170 175
Val Ile Gln Glu Lys Trp Pro Glu Val Asp Asp Asp Ser Ile Glu Asp
180 185 190
Leu Gly Glu Val Lys Lys
195
<210> 7
<211> 181
<212> PRT
<213> Homo sapiens
<400> 7
Met Phe Lys Lys Phe Asp Glu Lys Glu Asn Val Ser Asn Cys Ile Gln
1 5 10 15
Leu Lys Thr Ser Val Ile Lys Gly Ile Lys Asn Gln Leu Ile Glu Gln
20 25 30
Phe Pro Gly Ile Glu Pro Trp Leu Asn Gln Ile Met Pro Lys Lys Asp
35 40 45
Pro Val Lys Ile Val Arg Cys His Glu His Ile Glu Ile Leu Thr Val
50 55 60
Asn Gly Glu Leu Leu Phe Phe Arg Gln Arg Glu Gly Pro Phe Tyr Pro
65 70 75 80
Thr Leu Arg Leu Leu His Lys Tyr Pro Phe Ile Leu Pro His Gln Gln
85 90 95
Val Asp Lys Gly Ala Ile Lys Phe Val Leu Ser Gly Ala Asn Ile Met
100 105 110
Cys Pro Gly Leu Thr Ser Pro Gly Ala Lys Leu Tyr Pro Ala Ala Val
115 120 125
Asp Thr Ile Val Ala Ile Met Ala Glu Gly Lys Gln His Ala Leu Cys
130 135 140
Val Gly Val Met Lys Met Ser Ala Glu Asp Ile Glu Lys Val Asn Lys
145 150 155 160
Gly Ile Gly Ile Glu Asn Ile His Tyr Leu Asn Asp Gly Leu Trp His
165 170 175
Met Lys Thr Tyr Lys
180
<210> 8
<211> 172
<212> PRT
<213> Homo sapiens
<400> 8
Met Ile Ile Tyr Arg Asp Leu Ile Ser His Asp Glu Met Phe Ser Asp
1 5 10 15
Ile Tyr Lys Ile Arg Glu Ile Ala Asp Gly Leu Cys Leu Glu Val Glu
20 25 30
Gly Lys Met Val Ser Arg Thr Glu Gly Asn Ile Asp Asp Ser Leu Ile
35 40 45
Gly Gly Asn Ala Ser Ala Glu Gly Pro Glu Gly Glu Gly Thr Glu Ser
50 55 60
Thr Val Ile Thr Gly Val Asp Ile Val Met Asn His His Leu Gln Glu
65 70 75 80
Thr Ser Phe Thr Lys Glu Ala Tyr Lys Lys Tyr Ile Lys Asp Tyr Met
85 90 95
Lys Ser Ile Lys Gly Lys Leu Glu Glu Gln Arg Pro Glu Arg Val Lys
100 105 110
Pro Phe Met Thr Gly Ala Ala Glu Gln Ile Lys His Ile Leu Ala Asn
115 120 125
Phe Lys Asn Tyr Gln Phe Phe Ile Gly Glu Asn Met Asn Pro Asp Gly
130 135 140
Met Val Ala Leu Leu Asp Tyr Arg Glu Asp Gly Val Thr Pro Tyr Met
145 150 155 160
Ile Phe Phe Lys Asp Gly Leu Glu Met Glu Lys Cys
165 170
<210> 9
<211> 412
<212> PRT
<213> Homo sapiens
<400> 9
Pro Pro Lys Lys Gln Ala Gln Ala Gly Gly Ser Lys Lys Ala Glu Gln
1 5 10 15
Lys Lys Lys Glu Lys Ile Ile Glu Asp Lys Thr Phe Gly Leu Lys Asn
20 25 30
Lys Lys Gly Ala Lys Gln Gln Lys Phe Ile Lys Ala Val Thr His Gln
35 40 45
Val Lys Phe Gly Gln Gln Asn Pro Arg Gln Val Ala Gln Ser Glu Ala
50 55 60
Glu Lys Lys Leu Lys Lys Asp Asp Lys Lys Lys Glu Leu Gln Glu Leu
65 70 75 80
Asn Glu Leu Phe Lys Pro Val Val Ala Ala Gln Lys Ile Ser Lys Gly
85 90 95
Ala Asp Pro Lys Ser Val Val Cys Ala Phe Phe Lys Gln Gly Gln Cys
100 105 110
Thr Lys Gly Asp Lys Cys Lys Phe Ser His Asp Leu Thr Leu Glu Arg
115 120 125
Lys Cys Glu Lys Arg Ser Val Tyr Ile Asp Ala Arg Asp Glu Glu Leu
130 135 140
Glu Lys Asp Thr Met Asp Asn Trp Asp Glu Lys Lys Leu Glu Glu Val
145 150 155 160
Val Asn Lys Lys His Gly Glu Ala Glu Lys Lys Lys Pro Lys Thr Gln
165 170 175
Ile Val Cys Lys His Phe Leu Glu Ala Ile Glu Asn Asn Lys Tyr Gly
180 185 190
Trp Phe Trp Val Cys Pro Gly Gly Gly Asp Ile Cys Met Tyr Arg His
195 200 205
Ala Leu Pro Pro Gly Phe Val Leu Lys Lys Asp Lys Lys Lys Glu Glu
210 215 220
Lys Glu Asp Glu Ile Ser Leu Glu Asp Leu Ile Glu Arg Glu Arg Ser
225 230 235 240
Ala Leu Gly Pro Asn Val Thr Lys Ile Thr Leu Glu Ser Phe Leu Ala
245 250 255
Trp Lys Lys Arg Lys Arg Gln Glu Lys Ile Asp Lys Leu Glu Gln Asp
260 265 270
Met Glu Arg Arg Lys Ala Asp Phe Lys Ala Gly Lys Ala Leu Val Ile
275 280 285
Ser Gly Arg Glu Val Phe Glu Phe Arg Pro Glu Leu Val Asn Asp Asp
290 295 300
Asp Glu Glu Ala Asp Asp Thr Arg Tyr Thr Gln Gly Thr Gly Gly Asp
305 310 315 320
Glu Val Asp Asp Ser Val Ser Val Asn Asp Ile Asp Leu Ser Leu Tyr
325 330 335
Ile Pro Arg Asp Val Asp Glu Thr Gly Ile Thr Val Ala Ser Leu Glu
340 345 350
Arg Phe Ser Thr Tyr Thr Ser Asp Lys Asp Glu Asn Lys Leu Ser Glu
355 360 365
Ala Ser Gly Gly Arg Ala Glu Asn Gly Glu Arg Ser Asp Leu Glu Glu
370 375 380
Asp Asn Glu Arg Glu Gly Thr Glu Asn Gly Ala Ile Asp Ala Val Pro
385 390 395 400
Val Asp Glu Lys Ser Phe His Trp Arg Gly Phe Gly
405 410
<210> 10
<211> 269
<212> PRT
<213> Homo sapiens
<400> 10
Ala Cys Arg Pro Arg Ser Pro Pro Arg His Gln Ser Arg Cys Asp Gly
1 5 10 15
Asp Ala Ser Pro Pro Ser Pro Ala Arg Trp Ser Leu Gly Arg Lys Arg
20 25 30
Arg Ala Asp Gly Arg Arg Trp Arg Pro Glu Asp Ala Glu Glu Ala Glu
35 40 45
His Arg Gly Ala Glu Arg Arg Pro Glu Ser Phe Thr Thr Pro Glu Gly
50 55 60
Pro Lys Pro Arg Ser Arg Cys Ser Asp Trp Ala Ser Ala Val Glu Glu
65 70 75 80
Asp Glu Met Arg Thr Arg Val Asn Lys Glu Met Ala Arg Tyr Lys Arg
85 90 95
Lys Leu Leu Ile Asn Asp Phe Gly Arg Glu Arg Lys Ser Ser Ser Gly
100 105 110
Ser Ser Asp Ser Lys Glu Ser Met Ser Thr Val Pro Ala Asp Phe Glu
115 120 125
Thr Asp Glu Ser Val Leu Met Arg Arg Gln Lys Gln Ile Asn Tyr Gly
130 135 140
Lys Asn Thr Ile Ala Tyr Asp Arg Tyr Ile Lys Glu Val Pro Arg His
145 150 155 160
Leu Arg Gln Pro Gly Ile His Pro Lys Thr Pro Asn Lys Phe Lys Lys
165 170 175
Tyr Ser Arg Arg Ser Trp Asp Gln Gln Ile Lys Leu Trp Lys Val Ala
180 185 190
Leu His Phe Trp Asp Pro Pro Ala Glu Glu Gly Cys Asp Leu Gln Glu
195 200 205
Ile His Pro Val Asp Leu Glu Ser Ala Glu Ser Ser Ser Glu Pro Gln
210 215 220
Thr Ser Ser Gln Asp Asp Phe Asp Val Tyr Ser Gly Thr Pro Thr Lys
225 230 235 240
Val Arg His Met Asp Ser Gln Val Glu Asp Glu Phe Asp Leu Glu Ala
245 250 255
Cys Leu Thr Glu Pro Leu Arg Asp Phe Ser Ala Met Ser
260 265
<210> 11
<211> 95
<212> PRT
<213> Homo sapiens
<400> 11
Pro Gly Pro Thr Pro Ser Gly Thr Asn Val Gly Ser Ser Gly Arg Ser
1 5 10 15
Pro Ser Lys Ala Val Ala Ala Arg Ala Ala Gly Ser Thr Val Arg Gln
20 25 30
Arg Lys Asn Ala Ser Cys Gly Thr Arg Ser Ala Gly Arg Thr Thr Ser
35 40 45
Ala Gly Thr Gly Gly Met Trp Arg Phe Tyr Thr Glu Asp Ser Pro Gly
50 55 60
Leu Lys Val Gly Pro Val Pro Val Leu Val Met Ser Leu Leu Phe Ile
65 70 75 80
Ala Ser Val Phe Met Leu His Ile Trp Gly Lys Tyr Thr Arg Ser
85 90 95
<210> 12
<211> 23
<212> PRT
<213> Homo sapiens
<400> 12
Val Gly Pro Val Pro Val Leu Val Met Ser Leu Leu Phe Ile Ala Ser
1 5 10 15
Val Phe Met Leu His Ile Trp
20
<210> 13
<211> 285
<212> PRT
<213> Homo sapiens
<400> 13
Arg Leu Leu Pro Arg Leu Leu Leu Leu Leu Leu Leu Val Phe Pro Ala
1 5 10 15
Thr Val Leu Phe Arg Gly Gly Pro Arg Gly Leu Leu Ala Val Ala Gln
20 25 30
Asp Leu Thr Glu Asp Glu Glu Thr Val Glu Asp Ser Ile Ile Glu Asp
35 40 45
Glu Asp Asp Glu Ala Glu Val Glu Glu Asp Glu Pro Thr Asp Leu Val
50 55 60
Glu Asp Lys Glu Glu Glu Asp Val Ser Gly Glu Pro Glu Ala Ser Pro
65 70 75 80
Ser Ala Asp Thr Thr Ile Leu Phe Val Lys Gly Glu Asp Phe Pro Ala
85 90 95
Asn Asn Ile Val Lys Phe Leu Val Gly Phe Thr Asn Lys Gly Thr Glu
100 105 110
Asp Phe Ile Val Glu Ser Leu Asp Ala Ser Phe Arg Tyr Pro Gln Asp
115 120 125
Tyr Gln Phe Tyr Ile Gln Asn Phe Thr Ala Leu Pro Leu Asn Thr Val
130 135 140
Val Pro Pro Gln Arg Gln Ala Thr Phe Glu Tyr Ser Phe Ile Pro Ala
145 150 155 160
Glu Pro Met Gly Gly Arg Pro Phe Gly Leu Val Ile Asn Leu Asn Tyr
165 170 175
Lys Asp Leu Asn Gly Asn Val Phe Gln Asp Ala Val Phe Asn Gln Thr
180 185 190
Val Thr Val Ile Glu Arg Glu Asp Gly Leu Asp Gly Glu Thr Ile Phe
195 200 205
Met Tyr Met Phe Leu Ala Gly Leu Gly Leu Leu Val Ile Val Gly Leu
210 215 220
His Gln Leu Leu Glu Ser Arg Lys Arg Lys Arg Pro Ile Gln Lys Val
225 230 235 240
Glu Met Gly Thr Ser Ser Gln Asn Asp Val Asp Met Ser Trp Ile Pro
245 250 255
Gln Glu Thr Leu Asn Gln Ile Asn Lys Ala Ser Pro Arg Arg Leu Pro
260 265 270
Arg Lys Arg Ala Gln Lys Arg Ser Val Gly Ser Asp Glu
275 280 285
<210> 14
<211> 23
<212> PRT
<213> Homo sapiens
<400> 14
Thr Ile Phe Met Tyr Met Phe Leu Ala Gly Leu Gly Leu Leu Val Ile
1 5 10 15
Val Gly Leu His Gln Leu Leu
20
<210> 15
<211> 609
<212> PRT
<213> Homo sapiens
<400> 15
Leu Asp Phe Phe Thr Ile Phe Ser Lys Gly Gly Leu Val Leu Trp Cys
1 5 10 15
Phe Gln Gly Val Ser Asp Ser Cys Thr Gly Pro Val Asn Ala Leu Ile
20 25 30
Arg Ser Val Leu Leu Gln Val Gly Phe Gln Lys Ile Leu Thr Leu Thr
35 40 45
Tyr Val Asp Lys Leu Ile Asp Asp Val His Arg Leu Phe Arg Asp Lys
50 55 60
Tyr Arg Thr Glu Ile Gln Gln Gln Ser Ala Leu Ser Leu Leu Asn Gly
65 70 75 80
Thr Phe Asp Phe Gln Asn Asp Phe Leu Arg Leu Leu Arg Glu Ala Glu
85 90 95
Glu Ser Ser Lys Ile Arg Ala Pro Thr Thr Met Lys Lys Phe Glu Asp
100 105 110
Ser Glu Lys Ala Lys Lys Pro Val Arg Ser Met Ile Glu Thr Arg Gly
115 120 125
Glu Lys Pro Lys Glu Lys Ala Lys Asn Ser Lys Lys Lys Gly Ala Lys
130 135 140
Lys Glu Gly Ser Asp Gly Pro Leu Ala Thr Ser Lys Pro Val Pro Ala
145 150 155 160
Glu Lys Ser Gly Leu Pro Val Gly Pro Glu Asn Gly Val Glu Leu Ser
165 170 175
Lys Glu Glu Leu Ile Arg Arg Lys Arg Glu Glu Phe Ile Gln Lys His
180 185 190
Gly Arg Gly Met Glu Lys Ser Asn Lys Ser Thr Lys Ser Asp Ala Pro
195 200 205
Lys Glu Lys Gly Lys Lys Ala Pro Arg Val Trp Glu Leu Gly Gly Cys
210 215 220
Ala Asn Lys Glu Val Leu Asp Tyr Ser Thr Pro Thr Thr Asn Gly Thr
225 230 235 240
Pro Glu Ala Ala Leu Ser Glu Asp Ile Asn Leu Ile Arg Gly Thr Gly
245 250 255
Ser Gly Gly Gln Leu Gln Asp Leu Asp Cys Ser Ser Ser Asp Asp Glu
260 265 270
Gly Ala Ala Gln Asn Ser Thr Lys Pro Ser Ala Thr Lys Gly Thr Leu
275 280 285
Gly Gly Met Phe Gly Met Leu Lys Gly Leu Val Gly Ser Lys Ser Leu
290 295 300
Ser Arg Glu Asp Met Glu Ser Val Leu Asp Lys Met Arg Asp His Leu
305 310 315 320
Ile Ala Lys Asn Val Ala Ala Asp Ile Ala Val Gln Leu Cys Glu Ser
325 330 335
Val Ala Asn Lys Leu Glu Gly Lys Val Met Gly Thr Phe Ser Thr Val
340 345 350
Thr Ser Thr Val Lys Gln Ala Leu Gln Glu Ser Leu Val Gln Ile Leu
355 360 365
Gln Pro Gln Arg Arg Val Asp Met Leu Arg Asp Ile Met Asp Ala Gln
370 375 380
Arg Arg Gln Arg Pro Tyr Val Val Thr Phe Cys Gly Val Asn Gly Val
385 390 395 400
Gly Lys Ser Thr Asn Leu Ala Lys Ile Ser Phe Trp Leu Leu Glu Asn
405 410 415
Gly Phe Ser Val Leu Ile Ala Ala Cys Asp Thr Phe Arg Ala Gly Ala
420 425 430
Val Glu Gln Leu Arg Thr His Thr Arg Arg Leu Ser Ala Leu His Pro
435 440 445
Pro Glu Lys His Gly Gly Arg Thr Met Val Gln Leu Phe Glu Lys Gly
450 455 460
Tyr Gly Lys Asp Ala Ala Gly Ile Ala Met Glu Ala Ile Ala Phe Ala
465 470 475 480
Arg Asn Gln Gly Phe Asp Val Val Leu Val Asp Thr Ala Gly Arg Met
485 490 495
Gln Asp Asn Ala Pro Leu Met Thr Ala Leu Ala Lys Leu Ile Thr Val
500 505 510
Asn Thr Pro Asp Leu Val Leu Phe Val Gly Glu Ala Leu Val Gly Asn
515 520 525
Glu Ala Val Asp Gln Leu Val Lys Phe Asn Arg Ala Leu Ala Asp His
530 535 540
Ser Met Ala Gln Thr Pro Arg Leu Ile Asp Gly Ile Val Leu Thr Lys
545 550 555 560
Phe Asp Thr Ile Asp Asp Lys Val Gly Ala Ala Ile Ser Met Thr Tyr
565 570 575
Ile Thr Ser Lys Pro Ile Val Phe Val Gly Thr Gly Gln Thr Tyr Cys
580 585 590
Asp Leu Arg Ser Leu Asn Ala Lys Ala Val Val Ala Ala Leu Met Lys
595 600 605
Ala
<210> 16
<211> 18
<212> PRT
<213> Homo sapiens
<400> 16
Ser Thr Leu Gly His Met Val Leu Phe Pro Val Trp Phe Leu Tyr Ser
1 5 10 15
Leu Leu
<210> 17
<211> 261
<212> PRT
<213> Homo sapiens
<400> 17
Asp Ile Tyr Asp Thr Gln Thr Leu Gly Val Val Val Phe Gly Gly Phe
1 5 10 15
Met Val Val Ser Ala Ile Gly Ile Phe Leu Val Ser Thr Phe Ser Met
20 25 30
Lys Glu Thr Ser Tyr Glu Glu Ala Leu Ala Asn Gln Arg Lys Glu Met
35 40 45
Ala Lys Thr His His Gln Lys Val Glu Lys Lys Lys Lys Glu Lys Thr
50 55 60
Val Glu Lys Lys Gly Lys Thr Lys Lys Lys Glu Glu Lys Pro Asn Gly
65 70 75 80
Lys Ile Pro Asp His Asp Pro Ala Pro Asn Val Thr Val Leu Leu Arg
85 90 95
Glu Pro Val Arg Ala Pro Ala Val Ala Val Ala Pro Thr Pro Val Gln
100 105 110
Pro Pro Ile Ile Val Ala Pro Val Ala Thr Val Pro Ala Met Pro Gln
115 120 125
Glu Lys Leu Ala Ser Ser Pro Lys Asp Lys Lys Lys Lys Glu Lys Lys
130 135 140
Val Ala Lys Val Glu Pro Ala Val Ser Ser Val Val Asn Ser Ile Gln
145 150 155 160
Val Leu Thr Ser Lys Ala Ala Ile Leu Glu Thr Ala Pro Lys Glu Gly
165 170 175
Arg Asn Thr Asp Val Ala Gln Ser Pro Glu Ala Pro Lys Gln Glu Ala
180 185 190
Pro Ala Lys Lys Lys Ser Gly Ser Lys Lys Lys Gly Pro Pro Asp Ala
195 200 205
Asp Gly Pro Leu Tyr Leu Pro Tyr Lys Thr Leu Val Ser Thr Val Gly
210 215 220
Ser Met Val Phe Asn Glu Gly Glu Ala Gln Arg Leu Ile Glu Ile Leu
225 230 235 240
Ser Glu Lys Ala Gly Ile Ile Gln Asp Thr Trp His Lys Ala Thr Gln
245 250 255
Lys Gly Asp Pro Val
260
<210> 18
<211> 23
<212> PRT
<213> Homo sapiens
<400> 18
Leu Gly Val Val Val Phe Gly Gly Phe Met Val Val Ser Ala Ile Gly
1 5 10 15
Ile Phe Leu Val Ser Thr Phe
20
<210> 19
<211> 30
<212> PRT
<213> Homo sapiens
<400> 19
Asp Ile Tyr Asp Thr Gln Thr Leu Gly Val Val Val Phe Gly Gly Phe
1 5 10 15
Met Val Val Ser Ala Ile Gly Ile Phe Leu Val Ser Thr Phe
20 25 30
<210> 20
<211> 4
<212> PRT
<213> Homo sapiens
<400> 20
Lys Asp Glu Leu
1
<210> 21
<211> 4
<212> PRT
<213> Homo sapiens
<400> 21
Lys Glu Glu Leu
1
<210> 22
<211> 19
<212> PRT
<213> Homo sapiens
<400> 22
Met Gly Trp Ser Cys Ile Ile Leu Phe Leu Val Ala Thr Ala Thr Gly
1 5 10 15
Ala His Ser
Claims (15)
- 표적 mRNA로부터의 단백질 발현량을 향상시키기 위한 융합 단백질로서,
상기 융합 단백질은
(A) mRNA로부터의 단백질 발현량을 향상시키는 1개 이상의 기능적 도메인, 및
(B) 표적 mRNA에 대하여 RNA 염기 선택적으로 또는 RNA 염기서열 특이적으로 결합할 수 있는 폴리펩티드 모이어티
를 포함하며,
상기 (B)의 폴리펩티드 모이어티는 식 1로 표시되는, 30 내지 38개의 아미노산 길이의 폴리펩티드로 이루어지는 PPR 모티프를 1개 이상 포함하는 폴리펩티드 모이어티이고;
(식 1)
(식 1에서,
Helix A는 12개의 아미노산 길이의 a-나선 구조를 형성할 수 있는 모이어티이고, 식 2로 표시되며,
(식 2)
식 2에서, A1 내지 A12는 각각 독립적으로 아미노산을 나타내고;
X는 존재하지 않거나, 또는 1 내지 9개의 아미노산 길이로 이루어지는 모이어티이고;
Helix B는 11 내지 13개의 아미노산 길이로 이루어지는 a-나선 구조를 형성할 수 있는 모이어티이고;
L은 2 내지 7개의 아미노산 길이의 식 3으로 표시되는 모이어티이고:
(식 3)
식 3에서, 각 아미노산은 "i"(-1), "ii"(-2)로 C 말단측으로부터 넘버링되며,
다만, Liii 내지 Lvii은 존재하지 않을 수 있음)
A1, A4 및 Lii의 세 개의 아미노산 조합 또는 A4 및 Lii의 두 개의 아미노산 조합은 표적 mRNA의 염기 또는 염기서열에 상응하는 것인 융합 단백질. - 제1항에 있어서,
상기 (B)의 폴리펩티드 모이어티는 상기 PPR 모티프를 2 내지 30개 포함하고, 상기 복수 개의 PPR 모티프는 표적 mRNA의 염기서열에 특이적으로 결합하도록 배열되는 것인 융합 단백질. - 제2항에 있어서,
상기 (B)의 폴리펩티드 모이어티는 상기 PPR 모티프를 5 내지 25개 포함하는 것인 융합 단백질. - 제1항 내지 제3항 중 어느 한 항에 있어서,
상기 (A)의 기능적 도메인은 상기 (B)의 폴리펩티드 모이어티의 N 말단측 및/또는 C 말단측에 결합되는 것인 융합 단백질. - 제1항 내지 제4항 중 어느 한 항에 있어서,
상기 (A)의 기능적 도메인은 mRNA로 리보솜을 유도하는 도메인, mRNA의 번역개시 또는 번역촉진과 관련된 도메인, mRNA의 핵 외로의 수송과 관련된 도메인, 소포체 막에 대한 결합과 관련된 도메인, 소포체 보유 신호(ER retention signal) 서열을 포함하는 도메인 및 소포체 신호 서열을 포함하는 도메인으로 이루어지는 군으로부터 선택되는 것인 융합 단백질. - 제5항에 있어서,
밀도 조절된 단백질(Density-regulated protein, DENR), 악성 T-세포 증폭된 서열 1(Malignant T-cell amplified sequence 1, MCT-1), 번역 제어된 종양 단백질(Translationally-controlled tumor protein, TPT1) 및 징크 핑거 CCCH-도메인(Zinc finger CCCH-domain, Lerepo4)로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 포함하는 도메인이고,
상기 mRNA의 번역개시 또는 번역촉진과 관련된 도메인은 eIF4E 및 eIF4G로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 mRNA의 핵 외로의 수송과 관련된 도메인은 스템-루프 결합 단백질(Stem -loop binding protein, SLBP)의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 소포체 막에 대한 결합과 관련된 도메인은 SEC61B, 트랜스로콘 관련 단백질 알파(Translocon associated protein(TRAP)-alpha), SR-알파, 시토크롬 b5 환원효소 3(Cytochrome b5 reductase 3, Dia1) 및 p180으로 이루어지는 군으로부터 선택되는 폴리펩티드의 전부 또는 기능적인 일부를 함유하는 도메인이고,
상기 소포체 보유 신호(ER retention signal) 서열은 KDEL(KEEL) 서열을 포함하는 신호 서열이거나, 또는
상기 소포체 신호 서열은 MGWSCIILFLVATATGAHS를 포함하는 신호 서열인 융합 단백질. - 제1항 내지 제6항 중 어느 한 항에 있어서,
상기 각각의 PPR 모티프에서의 A1, A4 및 Lii의 세 개의 아미노산 조합은;
PPR 모티프의 표적 염기가 A(아데닌)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 트레오닌, 아스파라긴), (페닐알라닌, 세린, 아스파라긴), (페닐알라닌, 트레오닌, 아스파라긴), (이소류신, 아스파라긴, 아스파르트산) 또는 (트레오닌, 트레오닌, 아스파라긴)이고;
PPR 모티프의 표적 염기가 G(구아닌)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (글루탐산, 글리신, 아스파르트산), (발린, 트레오닌, 아스파르트산), (리신, 트레오닌, 아스파르트산) 또는 (류신, 트레오닌, 아스파르트산)이고;
PPR 모티프의 표적 염기가 U(우라실)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 아스파라긴, 아스파르트산), (이소류신, 아스파라긴, 아스파라긴), (이소류신, 아스파라긴, 아스파르트산), (이소류신, 메티오닌, 아스파르트산), (페닐알라닌, 프롤린, 아스파르트산) 또는 (티로신, 프롤린, 아스파르트산)이거나; 또는
PPR 모티프의 표적 염기가 C(시토신)일 경우, A1, A4 및 Lii의 세 개의 아미노산 조합은 (A1, A4, Lii)의 순으로 (발린, 아스파라긴, 아스파라긴), (이소류신, 아스파라긴, 아스파라긴), (발린, 아스파라긴, 세린) 또는 (이소류신, 메티오닌, 아스파르트산)인 것인 융합 단백질. - 제1항 내지 제6항 중 어느 한 항에 있어서,
상기 각각의 PPR 모티프에서의 A4 및 Lii의 두 개의 아미노산 조합은;
PPR 모티프의 표적 염기가 A(아데닌)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (트레오닌, 아스파라긴), (세린, 아스파라긴) 또는 (글리신, 아스파라긴)이고;
PPR 모티프의 표적 염기가 G(구아닌)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (트레오닌, 아스파르트산) 또는 (글리신, 아스파르트산)이고;
PPR 모티프의 표적 염기가 U(우라실)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (아스파라긴, 아스파르트산), (프롤린, 아스파르트산), (메티오닌, 아스파르트산) 또는 (발린, 트레오닌)이고;
PPR 모티프의 표적 염기가 C(시토신)일 경우, A4 및 Lii의 두 개의 아미노산 조합은 (A4, Lii)의 순으로 (아스파라긴, 아스파라긴), (아스파라긴, 세린) 또는 (류신, 아스파르트산)인 것인 융합 단백질. - 제1항 내지 제8항 중 어느 한 항에 따른 융합 단백질을 암호화하는 핵산.
- 제9항에 따른 핵산을 포함하는 벡터.
- 제10항에 있어서,
벡터는 발현 벡터인 것인 벡터. - 세포 내에서 표적 mRNA로부터의 단백질 발현량을 향상시키는 방법으로서,
제1항 내지 제8항 중 어느 한 항에 따른 융합 단백질, 또는 제10항 또는 제11항에 따른 벡터를 준비하는 단계; 및
상기 융합 단백질 또는 벡터를 세포 내로 도입하는 단계
를 포함하는 방법. - 제12항에 있어서,
세포는 진핵 세포인 것인 방법. - 제13항에 있어서,
세포는 동물 세포인 것인 방법. - 제14항에 있어서,
상기 동물 세포는 인간 세포인 것인 방법.
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