JP2003525593A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2003525593A5 JP2003525593A5 JP2001506798A JP2001506798A JP2003525593A5 JP 2003525593 A5 JP2003525593 A5 JP 2003525593A5 JP 2001506798 A JP2001506798 A JP 2001506798A JP 2001506798 A JP2001506798 A JP 2001506798A JP 2003525593 A5 JP2003525593 A5 JP 2003525593A5
- Authority
- JP
- Japan
- Prior art keywords
- seq
- nucleic acid
- acid molecule
- polypeptide
- corynebacterium
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 150000007523 nucleic acids Chemical class 0.000 description 23
- 108020004707 nucleic acids Proteins 0.000 description 23
- 229920001184 polypeptide Polymers 0.000 description 18
- 150000001413 amino acids Chemical group 0.000 description 16
- 229920001850 Nucleic acid sequence Polymers 0.000 description 11
- 239000000126 substance Substances 0.000 description 9
- 230000000295 complement Effects 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 241000186216 Corynebacterium Species 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 4
- 241000186226 Corynebacterium glutamicum Species 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 241000186146 Brevibacterium Species 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 229940029983 VITAMINS Drugs 0.000 description 2
- 229940021016 Vitamin IV solution additives Drugs 0.000 description 2
- 150000005018 aminopurines Chemical class 0.000 description 2
- 150000005005 aminopyrimidines Chemical class 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- -1 cofactors Natural products 0.000 description 2
- 150000002009 diols Chemical class 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 125000003835 nucleoside group Chemical group 0.000 description 2
- 150000007524 organic acids Chemical class 0.000 description 2
- 235000005985 organic acids Nutrition 0.000 description 2
- 125000000830 polyketide group Chemical group 0.000 description 2
- 229930001119 polyketides Natural products 0.000 description 2
- 230000001105 regulatory Effects 0.000 description 2
- 235000003441 saturated fatty acids Nutrition 0.000 description 2
- 150000004671 saturated fatty acids Chemical class 0.000 description 2
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 2
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 2
- 239000011782 vitamin Substances 0.000 description 2
- 235000013343 vitamin Nutrition 0.000 description 2
- 229930003231 vitamins Natural products 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 1
- 229940009098 Aspartate Drugs 0.000 description 1
- 235000012539 Bacterium linens Nutrition 0.000 description 1
- 241000186310 Brevibacterium linens Species 0.000 description 1
- 241000186145 Corynebacterium ammoniagenes Species 0.000 description 1
- MTCFGRXMJLQNBG-UWTATZPHSA-N D-serine Chemical compound OC[C@@H](N)C(O)=O MTCFGRXMJLQNBG-UWTATZPHSA-N 0.000 description 1
- QIVBCDIJIAJPQS-SECBINFHSA-N D-tryptophane Chemical compound C1=CC=C2C(C[C@@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-SECBINFHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-UHFFFAOYSA-N DL-aspartic acid Chemical compound OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 description 1
- 206010013023 Diphtheria Diseases 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241001235200 Haemophilus influenzae Rd KW20 Species 0.000 description 1
- 229960000310 ISOLEUCINE Drugs 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 229960005190 Phenylalanine Drugs 0.000 description 1
- 241000187561 Rhodococcus erythropolis Species 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 241000319304 [Brevibacterium] flavum Species 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 229920003013 deoxyribonucleic acid Polymers 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
Description
【特許請求の範囲】
【請求項１】
配列番号がＳＥＱ ＩＤ ＮＯ：１３のヌクレオチド配列を含む単離された核酸分子、またはこのヌクレオチド配列に相補性を有する核酸分子。
【請求項２】
配列番号がＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含むポリペプチドをコードする単離された核酸分子、またはその相補体。
【請求項３】
配列番号がＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含むポリペプチドの自然に発生する対立性変異体をコードする単離された核酸分子、またはその相補体。
【請求項４】
配列番号がＳＥＱ ＩＤ ＮＯ：１３の全ヌクレオチド配列と少なくとも５０％の相同性を有するヌクレオチド配列を含む単離された核酸分子、またはその相補体。
【請求項５】
配列番号がＳＥＱ ＩＤ ＮＯ：１３のヌクレオチド配列の少なくとも１５の連続したヌクレオチドのフラグメントを含む単離された核酸分子、またはその相補体。
【請求項６】
配列番号がＳＥＱ ＩＤ ＮＯ：１４の全アミノ酸配列と少なくとも５０％の相同性を有するアミノ酸配列を含むポリペプチドをコードする単離された核酸分子、またはその相補体。
【請求項７】
請求項１〜６のいずれか１項に記載の核酸分子および異種ポリペプチドをコードするヌクレオチド配列を含む、単離された核酸分子。
【請求項８】
請求項１〜７のいずれか１項に記載の核酸分子を含むベクター。
【請求項９】
発現ベクターである請求項８に記載のベクター。
【請求項１０】
請求項９に記載の発現ベクターによりトランスフェクションされた宿主細胞。
【請求項１１】
前記細胞が微生物である請求項１０に記載の宿主細胞。
【請求項１２】
前記細胞が、コリネバクテリウム属またはブレビバクテリウム属に属する請求項１１に記載の宿主細胞。
【請求項１３】
前記核酸分子の発現により、前記細胞からのファインケミカルの製造が調節される請求項１０に記載の宿主細胞。
【請求項１４】
ファインケミカルが、有機酸、タンパク原アミノ酸および非タンパク原アミノ酸、プリンおよびピリミジン塩基、ヌクレオシド、ヌクレオチド、脂質、飽和および不飽和の脂肪酸、ジオール、炭水化物、芳香族化合物、ビタミン、補助因子、ポリケチド、および酵素からなる群より選択される請求項１３に記載の宿主細胞。
【請求項１５】
適当な培地中で請求項１０に記載の宿主細胞を培養し、これによりポリペプチドを製造することを含む、ポリペプチドの製造方法。
【請求項１６】
配列番号がＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含む単離されたポリペプチド。
【請求項１７】
配列番号がＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含むポリペプチドの自然に発生する対立性変異体を含む単離されたポリペプチド。
【請求項１８】
配列番号がＳＥＱ ＩＤ ＮＯ：１３の全ヌクレオチド配列と少なくとも５０％の相同性を有するヌクレオチド配列を含む核酸分子でコードされる単離されたポリペプチド。
【請求項１９】
配列番号がＳＥＱ ＩＤ ＮＯ：１４の全アミノ酸配列と少なくとも５０％の相同性を有するアミノ酸配列を含む単離されたポリペプチド。
【請求項２０】
配列番号がＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含むポリペプチドのフラグメントを含む単離されたポリペプチドであって、前記ポリペプチドのフラグメントがＳＥＱ ＩＤ ＮＯ：１４のアミノ酸配列を含むポリペプチドの生物活性を維持していることを特徴とする単離されたポリペプチド。
【請求項２１】
配列番号がＳＥＱ ＩＤ ＮＯ：１３のヌクレオチド配列を含む核酸分子によってコードされるアミノ酸配列を含む単離されたポリペプチド。
【請求項２２】
さらに異種アミノ酸配列を含む、請求項１６〜２１のいずれか１項に記載の単離されたポリペプチド。
【請求項２３】
請求項１０に記載の細胞を培養してファインケミカルを製造する、ファインケミカルの製造方法。
【請求項２４】
さらに培養物からファインケミカルを回収する工程を含む請求項２３に記載の方法。
【請求項２５】
細胞が、コリネバクテリウム属またはブレビバクテリウム属に属す請求項２３に記載の方法。
【請求項２６】
当該細胞が、コリネバクテリウム−グルタミカム, コリネバクテリウム−ヘルキュリス、コリネバクテリウム−リリウム、コリネバクテリウム−アセトアシドフィリウム、コリネバクテリウム−アセトグルタミカム、コリネバクテリウム−アセトフィリウム、コリネバクテリウム−アンモニアゲン、 コリネバクテリウム−フジオケンス、コリネバクテリウム−ニトリロフィリウス、 ブレビバクテリウム−アンモニアゲン、ブレビバクテリウム−ブタニカム、 ブレビバクテリウム−ジバリカツム、ブレビバクテリウム−フラバム、ブレビバクテリウム−ヘアリ、ブレビバクテリウム−ケトグルタミカム、ブレビバクテリウム−ケトソレダクタアム、ブレビバクテリウム−ラクトフェルメンツム、ブレビバクテリウム−リネンス、ブレビバクテリウム−パラフィノリツカム、および表３に記載の株からなる群より選択される請求項２３に記載の方法。
【請求項２７】
前記ベクターによる核酸分子の発現により、前記ファインケミカルの製造の調節される請求項２３に記載の方法。
【請求項２８】
当該ファインケミカルが、有機酸、タンパク質原アミノ酸および非タンパク質原アミノ酸、プリンおよびピリミジン塩基、ヌクレオシド、ヌクレオチド、脂質、飽和および不飽和の脂肪酸、ジオール、炭水化物、芳香族化合物、ビタミン、共同因子、ポリケチド、および酵素からなる群より選択される請求項２３に記載の方法。
【請求項２９】
ファインケミカルがアミノ酸である請求項２３に記載の方法。
【請求項３０】
アミノ酸が、リジン、グルタマート、グルタミン、アラニン、アスパルタート、グリシン、セリン、トレオニン、メチオニン、システイン、バリン、ロイシン、イソロイシン、アルギニン、プロリン、ヒスチジン、チロシン、フェニルアラニン、およびトリプトファンから成る群より選択される請求項２９に記載の方法。
【請求項３１】
請求項１〜６のいずれか１項に記載の核酸分子の含有によってゲノムＤＮＡが変異した細胞を培養する工程を含むファインケミカルの製造方法。
【請求項３２】
請求項１〜６のいずれか１項に記載の核酸分子の少なくとも１種又は請求項１６〜２１のいずれか１項に記載のポリペプチド分子の少なくとも１種の存在を検出し、これによりコリネバクテリウム−ジフテリアの存在または活性を検出する工程を含むコリネバクテリウム−ジフテリアの存在または活性の検出方法。
【請求項３３】
配列番号がＳＥＱ ＩＤ ＮＯ：１３の核酸分子を含み、核酸分子が混乱している宿主細胞。
【請求項３４】
配列番号がＳＥＱ ＩＤ ＮＯ：１３の核酸分子を含み、核酸分子がＳＥＱ ＩＤ ＮＯ：１３の配列に比較して１個以上の核酸で修飾されている宿主細胞。
【請求項３５】
配列番号がＳＥＱ ＩＤ ＮＯ：１３の核酸分子を含み、核酸分子の調節領域が、分子の野生型調節領域と関連して修飾されている宿主細胞。
[Claims]
(1)
An isolated nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 13, or a nucleic acid molecule having complementarity to this nucleotide sequence.
(2)
An isolated nucleic acid molecule encoding a polypeptide having the amino acid sequence of SEQ ID NO: 14, or its complement.
(3)
An isolated nucleic acid molecule encoding a naturally occurring allelic variant of a polypeptide having the amino acid sequence of SEQ ID NO: 14, or its complement.
(4)
An isolated nucleic acid molecule comprising a nucleotide sequence having at least 50% homology to the entire nucleotide sequence of SEQ ID NO: 13, or a complement thereof.
(5)
An isolated nucleic acid molecule comprising a fragment of at least 15 contiguous nucleotides of the nucleotide sequence of SEQ ID NO: 13, or its complement.
6.
An isolated nucleic acid molecule encoding a polypeptide comprising an amino acid sequence having at least 50% homology to the entire amino acid sequence of SEQ ID NO: 14, or a complement thereof.
7.
An isolated nucleic acid molecule comprising a nucleic acid molecule according to any one of claims 1 to 6 and a nucleotide sequence encoding a heterologous polypeptide.
Claim 8.
A vector comprising the nucleic acid molecule according to any one of claims 1 to 7.
9.
The vector according to claim 8, which is an expression vector.
10.
A host cell transfected with the expression vector according to claim 9.
11.
The host cell according to claim 10, wherein the cell is a microorganism.
12.
The host cell according to claim 11, wherein the cell belongs to the genus Corynebacterium or the genus Brevibacterium.
Claim 13
11. The host cell according to claim 10, wherein the expression of the nucleic acid molecule regulates the production of a fine chemical from the cell.
14.
Fine chemicals include organic acids, proteinogenic and non-proteinogenic amino acids, purine and pyrimidine bases, nucleosides, nucleotides, lipids, saturated and unsaturated fatty acids, diols, carbohydrates, aromatics, vitamins, cofactors, polyketides, and enzymes. 14. The host cell according to claim 13, wherein the host cell is selected from the group consisting of:
15.
A method for producing a polypeptide, comprising culturing the host cell according to claim 10 in a suitable medium and producing the polypeptide with the cultivation.
16.
An isolated polypeptide comprising the amino acid sequence of SEQ ID NO: 14.
17.
An isolated polypeptide comprising a naturally occurring allelic variant of a polypeptide having the amino acid sequence of SEQ ID NO: 14.
18.
An isolated polypeptide encoded by a nucleic acid molecule comprising a nucleotide sequence having a SEQ ID NO: at least 50% homology to the entire nucleotide sequence of SEQ ID NO: 13.
(19)
An isolated polypeptide comprising an amino acid sequence having a SEQ ID NO: at least 50% homology to the entire amino acid sequence of SEQ ID NO: 14.
20.
A biological activity of an isolated polypeptide comprising a fragment of a polypeptide comprising the amino acid sequence of SEQ ID NO: 14, wherein said fragment of said polypeptide comprises the amino acid sequence of SEQ ID NO: 14 An isolated polypeptide, characterized in that:
21.
An isolated polypeptide comprising an amino acid sequence encoded by a nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 13.
22.
22. The isolated polypeptide according to any one of claims 16 to 21, further comprising a heterologous amino acid sequence.
23.
A method for producing a fine chemical, comprising culturing the cell according to claim 10 to produce a fine chemical.
24.
24. The method of claim 23, further comprising the step of recovering the fine chemical from the culture.
25.
The method according to claim 23, wherein the cell belongs to the genus Corynebacterium or Brevibacterium.
26.
The cells are Corynebacterium-glutamicum, Corynebacterium-herculis, Corynebacterium-lilium, Corynebacterium-acetoacidophilium, Corynebacterium-acetoglutamicum, Corynebacterium-acetophyllium, Corynebacterium -Ammoniagen, Corynebacterium-fugiokens, Corynebacterium-nitrilofilius, Brevibacterium-ammonogen, Brevibacterium-butanicum, Brevibacterium-divacatum, Brevibacterium-flavum, Brevibacterium-hairy, Brevi Bacterium-ketoglutamicum, Brevibacterium-ketosoledactam, Brevibacterium-lactofermentum, Brevibacterium-linens, Brevibacte Um - para Fi Nori grab, and method of claim 23 which is selected from the group consisting of strains described in Table 3.
27.
24. The method of claim 23, wherein the expression of the nucleic acid molecule by the vector regulates the production of the fine chemical.
28.
The fine chemicals include organic acids, proteinogenic and non-proteinogenic amino acids, purine and pyrimidine bases, nucleosides, nucleotides, lipids, saturated and unsaturated fatty acids, diols, carbohydrates, aromatics, vitamins, cofactors, polyketides, and 24. The method according to claim 23, wherein the method is selected from the group consisting of enzymes.
29.
The method according to claim 23, wherein the fine chemical is an amino acid.
30.
The amino acid is selected from the group consisting of lysine, glutamate, glutamine, alanine, aspartate, glycine, serine, threonine, methionine, cysteine, valine, leucine, isoleucine, arginine, proline, histidine, tyrosine, phenylalanine, and tryptophan. Item 30. The method according to Item 29.
31.
A method for producing a fine chemical, comprising a step of culturing cells whose genomic DNA has been mutated by containing the nucleic acid molecule according to any one of claims 1 to 6.
32.
The presence of at least one of the nucleic acid molecules according to any one of claims 1 to 6 or at least one of the polypeptide molecules according to any one of claims 16 to 21, whereby the Corynebacterium is detected. A method for detecting the presence or activity of Corynebacterium diphtheria, comprising the step of detecting the presence or activity of Um-diphtheria.
33.
A host cell comprising the nucleic acid molecule of SEQ ID NO: 13, wherein the nucleic acid molecule is disrupted.
34.
A host cell comprising the nucleic acid molecule of SEQ ID NO: 13, wherein the nucleic acid molecule has been modified with one or more nucleic acids as compared to the sequence of SEQ ID NO: 13.
35.
A host cell comprising the nucleic acid molecule of SEQ ID NO: 13, wherein the regulatory region of the nucleic acid molecule has been modified in relation to the wild-type regulatory region of the molecule.
実施例３：ＤＮＡシーケンスとコンピューターによる機能解析 実施例２に記載されたゲノムライブラリーを標準的な方法、特にＡＢＩ３７７シーケンスマシーンを用いた鎖成長停止反応法（例えばFleischman,R.D.ら(1995)'Whole-genome Random Sequencing and Assembly of Haemophilus Influenzae Rd.',Science, 269:496-512参照）に従ったＤＮＡシーケンスに使用した。以下のヌクレオチド配列のシーケンスプライマーが使用された：5'-GGAAACAGTATGACCATG-3'（ＳＥＱ ＩＤ ＮＯ：３０５）または5'-GTAAAACGACGGCCAGT-3'（ＳＥＱ ＩＤ ＮＯ：３０６）。
Example 3: DNA sequence and functional analysis by computer The genomic library described in Example 2 was subjected to a standard method, in particular, a chain growth termination reaction method using an ABI377 sequence machine (for example, Fleischman, RD et al. (1995) 'Whole -genome Random Sequencing and Assembly of Haemophilus Influenzae Rd. ', Science, 269: 496-512). The following nucleotide sequence primers were used: 5'-GGAAACAGTATGACCATG-3 ' (SEQ ID NO: 305) or 5'-GTAAAACGACGGCCAGT-3' (SEQ ID NO: 306) .
Applications Claiming Priority (25)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14103199P | 1999-06-25 | 1999-06-25 | |
| US60/141,031 | 1999-06-25 | ||
| US14269299P | 1999-07-01 | 1999-07-01 | |
| DE19930429.7 | 1999-07-01 | ||
| DE19930429 | 1999-07-01 | ||
| US60/142,692 | 1999-07-01 | ||
| DE19931413 | 1999-07-08 | ||
| DE19931457 | 1999-07-08 | ||
| DE19931413.6 | 1999-07-08 | ||
| DE19931541.8 | 1999-07-08 | ||
| DE19931457.8 | 1999-07-08 | ||
| DE19931541 | 1999-07-08 | ||
| DE19932230 | 1999-07-09 | ||
| DE19932209 | 1999-07-09 | ||
| DE19932230.9 | 1999-07-09 | ||
| DE19932209.0 | 1999-07-09 | ||
| DE19932914.1 | 1999-07-14 | ||
| DE19932914 | 1999-07-14 | ||
| US15121499P | 1999-08-27 | 1999-08-27 | |
| US60/151,214 | 1999-08-27 | ||
| DE19940764 | 1999-08-27 | ||
| DE19940764.9 | 1999-08-27 | ||
| DE19941382 | 1999-08-31 | ||
| DE19941382.7 | 1999-08-31 | ||
| PCT/IB2000/000922 WO2001000804A2 (en) | 1999-06-25 | 2000-06-23 | Corynebacterium glutamicum genes encoding stress, resistance and tolerance proteins |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007121173A Division JP2007244392A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
| JP2007121127A Division JP2007244391A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2003525593A JP2003525593A (en) | 2003-09-02 |
| JP2003525593A5 true JP2003525593A5 (en) | 2007-06-28 |
Family
ID=27582954
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001506798A Pending JP2003525593A (en) | 1999-06-25 | 2000-06-23 | Stress, tolerance and tolerability proteins encoding Corynebacterium glutamicum gene |
| JP2007121127A Withdrawn JP2007244391A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
| JP2007121173A Withdrawn JP2007244392A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007121127A Withdrawn JP2007244391A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
| JP2007121173A Withdrawn JP2007244392A (en) | 1999-06-25 | 2007-05-01 | Stress, resistance and tolerance protein encoding corynebacterium glutamicum gene |
Country Status (12)
| Country | Link |
|---|---|
| EP (1) | EP1290178A2 (en) |
| JP (3) | JP2003525593A (en) |
| KR (4) | KR20070087094A (en) |
| AU (1) | AU783703B2 (en) |
| CA (1) | CA2380870A1 (en) |
| ES (1) | ES2184658T1 (en) |
| HU (1) | HUP0203340A2 (en) |
| MX (1) | MXPA01012844A (en) |
| PL (1) | PL359863A1 (en) |
| SK (1) | SK18882001A3 (en) |
| TR (1) | TR200103709T2 (en) |
| WO (1) | WO2001000804A2 (en) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR0012020A (en) | 1999-07-02 | 2002-07-02 | Ajinomoto Kk | Protein, and DNA |
| US6569650B1 (en) | 1999-08-13 | 2003-05-27 | Degussa Ag | Process for the fermentative preparation of metabolic products and for the nucleotide sequences encoding for the sod gene |
| EP1156115A1 (en) | 2000-05-12 | 2001-11-21 | Degussa AG | Corynebacterium glutamicum strain with enhanced secretion activity |
| DE10032350A1 (en) | 2000-07-04 | 2002-01-24 | Degussa | New coryneform bacterium in which the mdhA gene is attenuated, preferably eliminated, useful for fermentative production of L-amino acids such as L-lysine |
| CN100529081C (en) | 2000-08-10 | 2009-08-19 | 德古萨股份公司 | Nucleotide sequences which code for lysR2 gene |
| DE10042051A1 (en) * | 2000-08-26 | 2002-03-07 | Degussa | New nucleotide sequences coding for the cstA gene |
| WO2002018589A2 (en) * | 2000-09-02 | 2002-03-07 | Degussa Ag | Nucleotide sequence coding for the sigc gene of corynebacterium glutamicum |
| AU2001293723A1 (en) | 2000-09-09 | 2002-03-22 | Degussa A.G. | Nucleotide sequences coding for the dep33 gene |
| EP1315815B1 (en) | 2000-09-09 | 2007-04-18 | Degussa GmbH | Nucleotide sequences which code for the dep34 gene |
| US6759224B2 (en) | 2000-09-09 | 2004-07-06 | Degussa Ag | Nucleotide sequences which code for the sahH gene |
| DE10154181A1 (en) * | 2001-11-05 | 2003-05-15 | Basf Ag | Genes that code for stress resistance and tolerance proteins |
| DE10154180A1 (en) * | 2001-11-05 | 2003-05-15 | Basf Ag | genes which code for genetic stability, gene expression and folding proteins |
| WO2005014828A2 (en) * | 2003-08-01 | 2005-02-17 | Basf Plant Science Gmbh | Process for the production of fine chemicals in plants |
| US8008545B2 (en) | 2003-04-15 | 2011-08-30 | Basf Plant Science Gmbh | Process for the production of fine chemicals |
| US7468262B2 (en) | 2003-05-16 | 2008-12-23 | Ajinomoto Co., Inc. | Polynucleotides encoding useful polypeptides in corynebacterium glutamicum ssp. lactofermentum |
| DE10359660A1 (en) * | 2003-12-18 | 2005-07-28 | Basf Ag | Psod expression units |
| DE10359594A1 (en) | 2003-12-18 | 2005-07-28 | Basf Ag | PEF TU-expression units |
| US8728795B2 (en) | 2003-12-18 | 2014-05-20 | Basf Se | Pgro expression units |
| DE102004035065A1 (en) * | 2004-07-20 | 2006-02-16 | Basf Ag | P-ET-TS expression units |
| JP5537818B2 (en) * | 2008-03-04 | 2014-07-02 | 国立大学法人信州大学 | Method for producing useful substances |
| JPWO2010095642A1 (en) * | 2009-02-18 | 2012-08-23 | 国立大学法人信州大学 | Method for producing useful substances |
| KR101694850B1 (en) | 2014-10-08 | 2017-01-10 | 씨제이제일제당 주식회사 | Microorganism producing L-glutamine and process for preparing L-glutamine using the same |
| KR101941745B1 (en) * | 2016-07-20 | 2019-01-24 | 씨제이제일제당 (주) | Microorganisms having an acyltransferase activity and the use thereof |
| EP3456833A1 (en) | 2017-09-18 | 2019-03-20 | Evonik Degussa GmbH | Method for the fermentative production of l-amino acids |
| EP3467099A1 (en) | 2017-10-05 | 2019-04-10 | Evonik Degussa GmbH | Method for the fermentative production of l-amino acids |
| RU2019128538A (en) | 2018-09-26 | 2021-03-11 | Эвоник Оперейшенс ГмбХ | METHOD FOR ENZYMATIC PRODUCTION OF L-LYSINE |
| CN111088202B (en) * | 2019-12-25 | 2022-01-04 | 南京工业大学 | Recombinant corynebacterium glutamicum for producing lysine through biological film-forming continuous fermentation and construction method thereof |
| CN111909912B (en) * | 2020-09-11 | 2022-03-08 | 四川农业大学 | MAP3K-19 gene for improving high-temperature tolerance of rice in heading stage, protein obtained by encoding same and application thereof |
| WO2023165952A1 (en) * | 2022-03-01 | 2023-09-07 | Evonik Operations Gmbh | Biotechnological production of collagen proteins and bacterial collagen-like proteins by recombinant microorganisms |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2607827A2 (en) * | 1985-09-27 | 1988-06-10 | Pasteur Institut | DNA fragment comprising at least a portion of a gene for resistance to lincosamides and biochemical and biological applications. |
| IT1196453B (en) * | 1986-07-04 | 1988-11-16 | Sclavo Spa | CORYNEBACTERIUM DIPHTHERIAE DNA ELEMENT WITH TYPICAL PROPERTIES OF AN IS INSERTION ELEMENT |
| WO1988009819A2 (en) * | 1987-06-12 | 1988-12-15 | Massachusetts Institute Of Technology | C. glutamicum threonine biosynthetic pathway |
| MY113040A (en) * | 1994-02-24 | 2001-11-30 | Ajinomoto Kk | Novel gene derived from coryneform bacteria and use thereof |
| BR9810990A (en) * | 1997-07-09 | 2000-08-08 | Ajinomoto Kk | DNA-corineform bacteria, and processes to produce l-glutamic acid, and, to produce l-lysine and l-glutamic acid. |
-
2000
- 2000-06-23 WO PCT/IB2000/000922 patent/WO2001000804A2/en active Search and Examination
- 2000-06-23 MX MXPA01012844A patent/MXPA01012844A/en active IP Right Grant
- 2000-06-23 TR TR2001/03709T patent/TR200103709T2/en unknown
- 2000-06-23 PL PL00359863A patent/PL359863A1/en unknown
- 2000-06-23 CA CA002380870A patent/CA2380870A1/en not_active Abandoned
- 2000-06-23 ES ES00944135T patent/ES2184658T1/en active Pending
- 2000-06-23 AU AU58369/00A patent/AU783703B2/en not_active Ceased
- 2000-06-23 HU HU0203340A patent/HUP0203340A2/en unknown
- 2000-06-23 SK SK1888-2001A patent/SK18882001A3/en not_active Application Discontinuation
- 2000-06-23 EP EP00944135A patent/EP1290178A2/en not_active Withdrawn
- 2000-06-23 KR KR1020077016198A patent/KR20070087094A/en not_active Application Discontinuation
- 2000-06-23 KR KR1020017016588A patent/KR100834986B1/en not_active IP Right Cessation
- 2000-06-23 KR KR1020077016199A patent/KR20070087095A/en not_active Application Discontinuation
- 2000-06-23 JP JP2001506798A patent/JP2003525593A/en active Pending
- 2000-06-23 KR KR1020067022892A patent/KR100878335B1/en not_active IP Right Cessation
-
2007
- 2007-05-01 JP JP2007121127A patent/JP2007244391A/en not_active Withdrawn
- 2007-05-01 JP JP2007121173A patent/JP2007244392A/en not_active Withdrawn
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2003525593A5 (en) | ||
| JP2003517291A5 (en) | ||
| JP2004534501A5 (en) | ||
| JP2004512808A5 (en) | ||
| JP2006271389A5 (en) | ||
| JP2006141405A5 (en) | ||
| KR100337959B1 (en) | Mutant Phosphoenolpyruvate Carboxylases, Genes and Amino Acids | |
| JP2003512024A5 (en) | ||
| US8604180B2 (en) | DNA fragment having promoter function | |
| JP5214633B2 (en) | L-arginine producing Corynebacterium glutamicum mutant and method for producing the same | |
| JP2018530320A (en) | Polymerase enzyme | |
| RU2007101915A (en) | CORYNEBACTERIUM GLUTAMICUM GENES CODING PROTEINS PARTICIPATING IN CARBON METABOLISM AND ENERGY PRODUCTION | |
| CA2216172A1 (en) | Process for producing nucleic acids | |
| CN115044521B (en) | Corynebacterium glutamicum mutant strain having improved L-lysine productivity and method for producing L-lysine using same | |
| CN115500080A (en) | Novel bifunctional methylenetetrahydrofolate dehydrogenase/methylenetetrahydrofolate cyclohydrolase variants and methods of producing XMP or GMP using the same | |
| RU2007110796A (en) | CORYNEBACTERIUM GLUTAMICUM GENES ENCODING PROTEINS OF THE PHOSPHOENOLPIRATUAT-SUGAR-PHOSPHOTHANOSTRASE | |
| RU2005120506A (en) | CORYNEBACTERIUM GLUTAMICUM GENES ENCODING PROTEINS OF METABOLIC WAYS | |
| CN115449519B (en) | Polynucleotide having promoter activity based on dapB gene and use thereof | |
| RU2007110850A (en) | Corynebacterium glutamicum genes encoding proteins of resistance and tolerance to stress | |
| CN117264034B (en) | BBD29_09715 gene mutant and application thereof in preparation of L-glutamic acid | |
| RU2005120505A (en) | CORYNEBACTERIUM GLUTAMICUM GENES ENCODING PROTEINS PARTICIPATING IN MEMBRANE SYNTHESIS AND MEMBRANE TRANSPORT | |
| JPH08196280A (en) | Sucrose gene originated from coryneform bacterium and its utilization | |
| RU2007110849A (en) | Corynebacterium glutamicum genes encoding proteins of the phosphoenolpyruvate-sugar-phosphorus transferase system | |
| RU2002101730A (en) | CORYNEBACTERIUM GLUTAMICUM GENES ENCODING PROTEINS OF RESISTANCE AND TOLERANCE TO STRESS | |
| RU2002102452A (en) | CORYNEBACTERIUM GLUTAMICUM genes encoding proteins of the phosphoenolpyruvate-sugar-phosphotransferase system |