NO309200B1 - Genledersekvens som induserer en post-translasjonell modifikasjon av polypeptider i bakterier og polypeptidsekvens - Google Patents
Genledersekvens som induserer en post-translasjonell modifikasjon av polypeptider i bakterier og polypeptidsekvens Download PDFInfo
- Publication number
- NO309200B1 NO309200B1 NO905638A NO905638A NO309200B1 NO 309200 B1 NO309200 B1 NO 309200B1 NO 905638 A NO905638 A NO 905638A NO 905638 A NO905638 A NO 905638A NO 309200 B1 NO309200 B1 NO 309200B1
- Authority
- NO
- Norway
- Prior art keywords
- aaa
- sequence
- gat
- aca
- tca
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 62
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 29
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 25
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 21
- 230000004481 post-translational protein modification Effects 0.000 title claims abstract description 21
- 241000894006 Bacteria Species 0.000 title claims abstract description 10
- 150000001413 amino acids Chemical class 0.000 claims abstract description 30
- 108010076504 Protein Sorting Signals Proteins 0.000 claims abstract description 4
- 102000004169 proteins and genes Human genes 0.000 claims description 31
- 239000002243 precursor Substances 0.000 claims description 23
- 108010053775 Nisin Proteins 0.000 claims description 20
- NVNLLIYOARQCIX-MSHCCFNRSA-N Nisin Chemical compound N1C(=O)[C@@H](CC(C)C)NC(=O)C(=C)NC(=O)[C@@H]([C@H](C)CC)NC(=O)[C@@H](NC(=O)C(=C/C)/NC(=O)[C@H](N)[C@H](C)CC)CSC[C@@H]1C(=O)N[C@@H]1C(=O)N2CCC[C@@H]2C(=O)NCC(=O)N[C@@H](C(=O)N[C@H](CCCCN)C(=O)N[C@@H]2C(NCC(=O)N[C@H](C)C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCSC)C(=O)NCC(=O)N[C@H](CS[C@@H]2C)C(=O)N[C@H](CC(N)=O)C(=O)N[C@H](CCSC)C(=O)N[C@H](CCCCN)C(=O)N[C@@H]2C(N[C@H](C)C(=O)N[C@@H]3C(=O)N[C@@H](C(N[C@H](CC=4NC=NC=4)C(=O)N[C@H](CS[C@@H]3C)C(=O)N[C@H](CO)C(=O)N[C@H]([C@H](C)CC)C(=O)N[C@H](CC=3NC=NC=3)C(=O)N[C@H](C(C)C)C(=O)NC(=C)C(=O)N[C@H](CCCCN)C(O)=O)=O)CS[C@@H]2C)=O)=O)CS[C@@H]1C NVNLLIYOARQCIX-MSHCCFNRSA-N 0.000 claims description 18
- 239000004309 nisin Substances 0.000 claims description 18
- 235000010297 nisin Nutrition 0.000 claims description 18
- 108010082567 subtilin Proteins 0.000 claims description 18
- 239000012634 fragment Substances 0.000 claims description 15
- RKLXDNHNLPUQRB-TVJUEJKUSA-N chembl564271 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]2C(C)SC[C@H](N[C@@H](CC(N)=O)C(=O)NC(=O)[C@@H](NC2=O)CSC1C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NC(=C)C(=O)N[C@@H](CCCCN)C(O)=O)NC(=O)[C@H]1NC(=O)C(=C\C)/NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]2NC(=O)CNC(=O)[C@@H]3CCCN3C(=O)[C@@H](NC(=O)[C@H]3N[C@@H](CC(C)C)C(=O)NC(=O)C(=C)NC(=O)CC[C@H](NC(=O)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC=4C5=CC=CC=C5NC=4)CSC3)C(O)=O)C(C)SC2)C(C)C)C(C)SC1)C1=CC=CC=C1 RKLXDNHNLPUQRB-TVJUEJKUSA-N 0.000 claims description 12
- 230000004048 modification Effects 0.000 claims description 9
- 238000012986 modification Methods 0.000 claims description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 5
- 230000001939 inductive effect Effects 0.000 claims description 3
- NZGRHTKZFSVPAN-BIIVOSGPSA-N Ala-Ser-Pro Chemical compound C[C@@H](C(=O)N[C@@H](CO)C(=O)N1CCC[C@@H]1C(=O)O)N NZGRHTKZFSVPAN-BIIVOSGPSA-N 0.000 claims 1
- BXUHCIXDSWRSBS-CIUDSAMLSA-N Asn-Leu-Asp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O BXUHCIXDSWRSBS-CIUDSAMLSA-N 0.000 claims 1
- KGHLGJAXYSVNJP-WHFBIAKZSA-N Asp-Ser-Gly Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CO)C(=O)NCC(O)=O KGHLGJAXYSVNJP-WHFBIAKZSA-N 0.000 claims 1
- QIJVAFLRMVBHMU-KKUMJFAQSA-N Lys-Asp-Phe Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O QIJVAFLRMVBHMU-KKUMJFAQSA-N 0.000 claims 1
- DBMLDOWSVHMQQN-XGEHTFHBSA-N Met-Ser-Thr Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(O)=O DBMLDOWSVHMQQN-XGEHTFHBSA-N 0.000 claims 1
- 108010079364 N-glycylalanine Proteins 0.000 claims 1
- CRJZZXMAADSBBQ-SRVKXCTJSA-N Ser-Lys-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CO CRJZZXMAADSBBQ-SRVKXCTJSA-N 0.000 claims 1
- NZYNRRGJJVSSTJ-GUBZILKMSA-N Val-Ser-Val Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(O)=O NZYNRRGJJVSSTJ-GUBZILKMSA-N 0.000 claims 1
- VPZXBVLAVMBEQI-UHFFFAOYSA-N glycyl-DL-alpha-alanine Natural products OC(=O)C(C)NC(=O)CN VPZXBVLAVMBEQI-UHFFFAOYSA-N 0.000 claims 1
- 238000000034 method Methods 0.000 abstract description 17
- 235000018102 proteins Nutrition 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 22
- 108020004414 DNA Proteins 0.000 description 13
- 239000000523 sample Substances 0.000 description 12
- 230000014509 gene expression Effects 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 238000009396 hybridization Methods 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 244000057717 Streptococcus lactis Species 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 5
- 229940041514 candida albicans extract Drugs 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 230000007246 mechanism Effects 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 239000012138 yeast extract Substances 0.000 description 5
- 235000014469 Bacillus subtilis Nutrition 0.000 description 4
- 108020004705 Codon Proteins 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 230000003115 biocidal effect Effects 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 125000001165 hydrophobic group Chemical group 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 238000002123 RNA extraction Methods 0.000 description 3
- 239000000853 adhesive Substances 0.000 description 3
- 230000001070 adhesive effect Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 210000003705 ribosome Anatomy 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- PAWSVPVNIXFKOS-IHWYPQMZSA-N (Z)-2-aminobutenoic acid Chemical compound C\C=C(/N)C(O)=O PAWSVPVNIXFKOS-IHWYPQMZSA-N 0.000 description 2
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- UQBOJOOOTLPNST-UHFFFAOYSA-N Dehydroalanine Chemical compound NC(=C)C(O)=O UQBOJOOOTLPNST-UHFFFAOYSA-N 0.000 description 2
- DWPCPZJAHOETAG-IMJSIDKUSA-N L-lanthionine Chemical compound OC(=O)[C@@H](N)CSC[C@H](N)C(O)=O DWPCPZJAHOETAG-IMJSIDKUSA-N 0.000 description 2
- 239000004677 Nylon Substances 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- 235000014897 Streptococcus lactis Nutrition 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 238000005273 aeration Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- -1 e-methyllanthionine Chemical compound 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- DWPCPZJAHOETAG-UHFFFAOYSA-N meso-lanthionine Natural products OC(=O)C(N)CSCC(N)C(O)=O DWPCPZJAHOETAG-UHFFFAOYSA-N 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 229920001778 nylon Polymers 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 239000012137 tryptone Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 241000193755 Bacillus cereus Species 0.000 description 1
- 108010023063 Bacto-peptone Proteins 0.000 description 1
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 1
- 229920000049 Carbon (fiber) Polymers 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 108020003215 DNA Probes Proteins 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 230000008836 DNA modification Effects 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- GDSYPXWUHMRTHT-UHFFFAOYSA-N Epidermin Natural products N#CCC(C)(C)OC1OC(CO)C(O)C(O)C1O GDSYPXWUHMRTHT-UHFFFAOYSA-N 0.000 description 1
- 239000004593 Epoxy Substances 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 239000007832 Na2SO4 Substances 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 101710149086 Nuclease S1 Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 101800001442 Peptide pr Proteins 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 229940024171 alpha-amylase Drugs 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000011114 ammonium hydroxide Nutrition 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000004917 carbon fiber Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 150000001945 cysteines Chemical class 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- 230000018044 dehydration Effects 0.000 description 1
- 238000006297 dehydration reaction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 229910000388 diammonium phosphate Inorganic materials 0.000 description 1
- 238000007337 electrophilic addition reaction Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- CXTXHTVXPMOOSW-JUEJINBGSA-N epidermin Chemical compound C([C@H]1C(=O)N[C@H](C(=O)N[C@@H](CSC[C@H](C(N[C@@H](CCCCN)C(=O)N1)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)[C@@H](C)CC)C(=O)N[C@H]1C(N2CCC[C@H]2C(=O)NCC(=O)N[C@@H](CS[C@H]1C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N\C(=C/C)C(=O)NCC(=O)N[C@H]1C(N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H]2C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@H](C(N\C=C/SC2)=O)CSC1)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 CXTXHTVXPMOOSW-JUEJINBGSA-N 0.000 description 1
- 108010064962 epidermin Proteins 0.000 description 1
- 125000003700 epoxy group Chemical group 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 108010009719 mutanolysin Proteins 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920000647 polyepoxide Polymers 0.000 description 1
- 239000003910 polypeptide antibiotic agent Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 239000011833 salt mixture Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 235000004400 serine Nutrition 0.000 description 1
- 150000003355 serines Chemical class 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 235000008521 threonine Nutrition 0.000 description 1
- 150000003588 threonines Chemical class 0.000 description 1
- 235000015193 tomato juice Nutrition 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 239000011592 zinc chloride Substances 0.000 description 1
- 235000005074 zinc chloride Nutrition 0.000 description 1
- JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
- C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/67—General methods for enhancing the expression
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/90—Fusion polypeptide containing a motif for post-translational modification
Landscapes
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Crystallography & Structural Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/214,959 US5218101A (en) | 1988-07-05 | 1988-07-05 | Leader sequence inducing a post-translational modification of polypeptides in bacteria, and gene therefor |
| PCT/US1989/002820 WO1990000558A1 (en) | 1988-07-05 | 1989-06-30 | Leader sequence inducing a post-translational modification of polypeptides in bacteria, and gene therefor |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO905638L NO905638L (no) | 1990-12-28 |
| NO905638D0 NO905638D0 (no) | 1990-12-28 |
| NO309200B1 true NO309200B1 (no) | 2000-12-27 |
Family
ID=22801074
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO905638A NO309200B1 (no) | 1988-07-05 | 1990-12-28 | Genledersekvens som induserer en post-translasjonell modifikasjon av polypeptider i bakterier og polypeptidsekvens |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US5218101A (de) |
| EP (1) | EP0423224B1 (de) |
| JP (2) | JP3326172B2 (de) |
| KR (1) | KR0137961B1 (de) |
| AT (1) | ATE175417T1 (de) |
| AU (1) | AU640110B2 (de) |
| CA (1) | CA1339414C (de) |
| DE (2) | DE68928899T4 (de) |
| DK (1) | DK191D0 (de) |
| IL (1) | IL90832A (de) |
| NO (1) | NO309200B1 (de) |
| NZ (1) | NZ229538A (de) |
| WO (1) | WO1990000558A1 (de) |
| ZA (1) | ZA894721B (de) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5516682A (en) * | 1988-07-05 | 1996-05-14 | University Of Maryland | Subtilin variant of enhanced stability and activity |
| US5348881A (en) * | 1990-03-13 | 1994-09-20 | Quest International Flavors & Good Ingredients Company, Division Of Indopco, Inc. | Multiple bacteriocin producing lactococcus and compositions |
| NL9000753A (nl) * | 1990-03-30 | 1991-10-16 | Nl Zuivelonderzoek Inst | Dna-fragment, ten minste coderend voor een deel van het extracellulaire eiwit met een schijnbaar molecuulgewicht van 60 kda van lactococcus lactis stammen zoals de lactococcus lactis ssp. lactis stam mg1363, combinaties hiervan met voor homologe of heterologe eiwitten coderende dna-sequenties alsmede de hiermee verkregen homologe en heterologe eiwitten. |
| DK0579730T3 (da) * | 1991-04-11 | 2003-03-31 | Stichting Nl I Voor Zuivelonde | Nisin A-lignende lantibiotika, mælkesyrebakterie der producerer sådanne lantibiotika, fremgangsmåde til konstruktion af sådanne mælkesyrebakterier og fremgangsmåde til konservering . . . |
| US5861376A (en) * | 1991-07-01 | 1999-01-19 | Quest International Flavors & Food Ingredients Company, Division Of Indopco, Inc. | Synthetically derived peptide |
| GB9207267D0 (en) * | 1992-04-02 | 1992-05-13 | Agricultural & Food Res | Nisins |
| DE69433357T2 (de) * | 1994-09-12 | 2004-09-09 | Aventis Pharma Deutschland Gmbh | Rekombinantes Mersacidin und Verfahren zu seiner Herstellung |
| US5919695A (en) * | 1997-04-22 | 1999-07-06 | Quest International, B.V. | Method and culture for inhibiting undesired microorganisms with culture of Bacillus subtilis |
| AU8484798A (en) * | 1997-07-18 | 1999-02-10 | University Of Maryland | Sublancin lantibiotic produced by (bacillus subtilis) 168 |
| US6953683B2 (en) * | 1997-07-18 | 2005-10-11 | University Of Maryland | Compositions and methods of inhibiting bacterial spore germination |
| CA2356955A1 (en) * | 1998-12-24 | 2000-07-06 | University Of Maryland | Stable subtilin and methods of manufacture |
| US6759205B2 (en) | 2000-06-29 | 2004-07-06 | University Of Maryland | Construction of a strain of Bacillus subtilis 168 that displays the sublancin lantibiotic on the surface of the cell |
| US7033766B2 (en) * | 2000-06-29 | 2006-04-25 | University Of Maryland Office Of Technology Commercialization | Construction and screening of lantibody display libraries |
| US6846804B2 (en) * | 2000-06-29 | 2005-01-25 | University Of Maryland, College Park Office Of Technology Commercialization | Construction of a structural variant of sublancin to facilitate its isolation and use in bioremediation of environmental contamination by gram-positive spore formers such as bacillus anthrasis |
| WO2003063887A1 (en) * | 2002-01-14 | 2003-08-07 | University Of Maryland, College Park | Compositions and method of inhibiting bacterial spore germination |
| US6861236B2 (en) * | 2002-05-24 | 2005-03-01 | Applied Nanosystems B.V. | Export and modification of (poly)peptides in the lantibiotic way |
| DE602005009738D1 (de) | 2004-12-07 | 2008-10-23 | Applied Nanosystems Bv | Verfahren zur herstellung und sekretion modifizierter peptide |
| EP1989219A1 (de) * | 2006-02-13 | 2008-11-12 | Boehringer Ingelheim Vetmedica Gmbh | Verfahren zur herstellung von lantibiotika |
| US7879973B2 (en) * | 2006-06-29 | 2011-02-01 | The Invention Science Fund I, Llc | Methods for arbitrary peptide synthesis |
| US7923533B2 (en) * | 2006-06-29 | 2011-04-12 | The Invention Science Fund I, Llc | Methods for arbitrary peptide synthesis |
| US7910695B2 (en) * | 2006-06-29 | 2011-03-22 | The Invention Science Fund I, Llc | Methods for arbitrary peptide synthesis |
| US7879975B2 (en) * | 2006-06-29 | 2011-02-01 | The Invention Science Fund I, Llc | Methods for arbitrary peptide synthesis |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4716115A (en) * | 1983-09-06 | 1987-12-29 | Microlife Technics, Inc. | Derived nisin producing microorganisms, method of production and use and products obtained thereby |
-
1988
- 1988-07-05 US US07/214,959 patent/US5218101A/en not_active Expired - Fee Related
-
1989
- 1989-06-14 NZ NZ229538A patent/NZ229538A/en unknown
- 1989-06-21 ZA ZA894721A patent/ZA894721B/xx unknown
- 1989-06-30 WO PCT/US1989/002820 patent/WO1990000558A1/en active IP Right Grant
- 1989-06-30 AT AT89908558T patent/ATE175417T1/de not_active IP Right Cessation
- 1989-06-30 DE DE68928899T patent/DE68928899T4/de not_active Expired - Lifetime
- 1989-06-30 JP JP50801189A patent/JP3326172B2/ja not_active Expired - Fee Related
- 1989-06-30 IL IL9083289A patent/IL90832A/en not_active IP Right Cessation
- 1989-06-30 EP EP89908558A patent/EP0423224B1/de not_active Expired - Lifetime
- 1989-06-30 AU AU39684/89A patent/AU640110B2/en not_active Ceased
- 1989-06-30 DE DE68928899A patent/DE68928899D1/de not_active Expired - Fee Related
- 1989-06-30 KR KR1019900700460A patent/KR0137961B1/ko not_active IP Right Cessation
- 1989-07-04 CA CA000604753A patent/CA1339414C/en not_active Expired - Fee Related
-
1990
- 1990-12-28 NO NO905638A patent/NO309200B1/no not_active IP Right Cessation
-
1991
- 1991-01-02 DK DK000191A patent/DK191D0/da not_active Application Discontinuation
-
2001
- 2001-11-08 JP JP2001343857A patent/JP3418388B2/ja not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| NO905638L (no) | 1990-12-28 |
| WO1990000558A1 (en) | 1990-01-25 |
| DE68928899T4 (de) | 1999-11-25 |
| EP0423224A4 (en) | 1991-11-06 |
| DK191A (da) | 1991-01-02 |
| ZA894721B (en) | 1990-03-28 |
| DK191D0 (da) | 1991-01-02 |
| JP2002191383A (ja) | 2002-07-09 |
| KR0137961B1 (ko) | 1998-04-30 |
| CA1339414C (en) | 1997-09-02 |
| JP3418388B2 (ja) | 2003-06-23 |
| EP0423224A1 (de) | 1991-04-24 |
| NO905638D0 (no) | 1990-12-28 |
| ATE175417T1 (de) | 1999-01-15 |
| US5218101A (en) | 1993-06-08 |
| KR900701819A (ko) | 1990-12-04 |
| IL90832A0 (en) | 1990-01-18 |
| AU3968489A (en) | 1990-02-05 |
| JPH03505670A (ja) | 1991-12-12 |
| IL90832A (en) | 1995-06-29 |
| AU640110B2 (en) | 1993-08-19 |
| NZ229538A (en) | 1992-01-29 |
| DE68928899T2 (de) | 1999-08-12 |
| JP3326172B2 (ja) | 2002-09-17 |
| DE68928899D1 (de) | 1999-02-18 |
| EP0423224B1 (de) | 1999-01-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO309200B1 (no) | Genledersekvens som induserer en post-translasjonell modifikasjon av polypeptider i bakterier og polypeptidsekvens | |
| Buchman et al. | Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic. | |
| Banerjee et al. | Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. | |
| Zalacain et al. | Nucleotide sequence of tbe hygromycin B phosphotransferase gene from Streptomyces hygroscopicus | |
| US5885811A (en) | Leader sequence inducing a post-translational modification of polypeptides in bacteria gene therefor and subtilin variant of enhanced stability and activity | |
| CA2185343A1 (en) | Enhanced secretion of polypeptides | |
| KR20010013540A (ko) | 초내열성 프로테아제 발현계 | |
| Nagasawa et al. | Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli | |
| HU214368B (hu) | Eljárás új hirudinszármazék előállítására | |
| WO1993024631A1 (en) | PRODUCTION OF STREPTAVIDIN FROM $i(BACILLUS SUBTILIS) | |
| EP0614982B1 (de) | Rekombinantes Vektor für die exozelluläre Verwendung von in Bacillus Subtilis exprimierten einkettigen Antikörpern | |
| CA2081704C (en) | Biosynthetic process for the preparation of lantibiotics | |
| AU655312B2 (en) | Isolation and characterization of a novel protease from streptomyces lividans | |
| US5843709A (en) | Biosynthetic process for the preparation of chemical compounds | |
| CA1275953C (en) | Recombinant materials and methods for producing human connective tissue-activating peptide-iii and analogs thereof | |
| EP0182562B1 (de) | Verfahren zur thermoinduzierbaren Genexpression in grampositiven Bakterien, Bacillus subtilis Stämme, die Plasmide enthalten, die eine solche Expression induzieren und portable Vektor-Systeme | |
| EP0342658B1 (de) | Biosynthetisches Verfahren zur Herstellung von chemischen Verbindungen | |
| HU204090B (en) | Process for producing and using new gene marked by t1rb, ensuring tylosin resistance and applicable within the domain of streptomyces and other microorganisms | |
| US5660999A (en) | P0438, a new calcium-regulated promoter |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |