LT3133B - Po438, a new calcium-regulated promotor - Google Patents
Po438, a new calcium-regulated promotor Download PDFInfo
- Publication number
- LT3133B LT3133B LTIP237A LTIP237A LT3133B LT 3133 B LT3133 B LT 3133B LT IP237 A LTIP237 A LT IP237A LT IP237 A LTIP237 A LT IP237A LT 3133 B LT3133 B LT 3133B
- Authority
- LT
- Lithuania
- Prior art keywords
- dna sequence
- streptomyces
- promoter
- sequence
- polypeptide
- Prior art date
Links
- 239000011575 calcium Substances 0.000 title claims abstract description 11
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 title claims abstract description 10
- 229910052791 calcium Inorganic materials 0.000 title claims abstract description 10
- 230000001105 regulatory effect Effects 0.000 title claims abstract description 8
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 46
- 241000187747 Streptomyces Species 0.000 claims abstract description 35
- 108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 26
- 230000014509 gene expression Effects 0.000 claims abstract description 24
- 229920001184 polypeptide Polymers 0.000 claims abstract description 23
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 23
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 23
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 21
- 238000000034 method Methods 0.000 claims abstract description 11
- 239000012634 fragment Substances 0.000 claims description 34
- 238000010367 cloning Methods 0.000 claims description 13
- 230000000694 effects Effects 0.000 claims description 8
- 239000002773 nucleotide Substances 0.000 claims description 4
- 125000003729 nucleotide group Chemical group 0.000 claims description 4
- 239000013611 chromosomal DNA Substances 0.000 claims description 2
- 241000272525 Anas platyrhynchos Species 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 abstract description 24
- 108090000790 Enzymes Proteins 0.000 abstract description 24
- 108020004414 DNA Proteins 0.000 abstract description 22
- 239000013598 vector Substances 0.000 abstract description 13
- 230000001965 increasing effect Effects 0.000 abstract description 5
- 238000004519 manufacturing process Methods 0.000 abstract description 4
- 230000003248 secreting effect Effects 0.000 abstract description 2
- 239000013612 plasmid Substances 0.000 description 22
- 229940088598 enzyme Drugs 0.000 description 21
- 241000187398 Streptomyces lividans Species 0.000 description 19
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 15
- 239000002609 medium Substances 0.000 description 12
- 230000001413 cellular effect Effects 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 108010028143 Dioxygenases Proteins 0.000 description 9
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 8
- 239000001110 calcium chloride Substances 0.000 description 8
- 229910001628 calcium chloride Inorganic materials 0.000 description 8
- 235000011148 calcium chloride Nutrition 0.000 description 8
- 101000796211 Streptomyces antibioticus Tyrosinase cofactor Proteins 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 230000028327 secretion Effects 0.000 description 7
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 6
- 102000016680 Dioxygenases Human genes 0.000 description 6
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 6
- 101710163270 Nuclease Proteins 0.000 description 6
- 229910001424 calcium ion Inorganic materials 0.000 description 6
- 101150110704 melC2 gene Proteins 0.000 description 6
- 239000004382 Amylase Substances 0.000 description 5
- 108010065511 Amylases Proteins 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 102000013142 Amylases Human genes 0.000 description 4
- 229930193140 Neomycin Natural products 0.000 description 4
- 235000019418 amylase Nutrition 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 229960004927 neomycin Drugs 0.000 description 4
- 229920002477 rna polymer Polymers 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 108010025815 Kanamycin Kinase Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108060008724 Tyrosinase Proteins 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 239000001307 helium Substances 0.000 description 3
- 229910052734 helium Inorganic materials 0.000 description 3
- SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 101150000461 saf gene Proteins 0.000 description 3
- 230000004936 stimulating effect Effects 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 241001045988 Neogene Species 0.000 description 2
- 241000589776 Pseudomonas putida Species 0.000 description 2
- 108700005075 Regulator Genes Proteins 0.000 description 2
- 241000186988 Streptomyces antibioticus Species 0.000 description 2
- 102000003425 Tyrosinase Human genes 0.000 description 2
- 108010045649 agarase Proteins 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 150000001768 cations Chemical class 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000013599 cloning vector Substances 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 239000006151 minimal media Substances 0.000 description 2
- 101150091879 neo gene Proteins 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 210000001938 protoplast Anatomy 0.000 description 2
- 230000008844 regulatory mechanism Effects 0.000 description 2
- 229930000044 secondary metabolite Natural products 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- DBTMGCOVALSLOR-UHFFFAOYSA-N 32-alpha-galactosyl-3-alpha-galactosyl-galactose Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(OC2C(C(CO)OC(O)C2O)O)OC(CO)C1O DBTMGCOVALSLOR-UHFFFAOYSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 101150076489 B gene Proteins 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 108020004256 Beta-lactamase Proteins 0.000 description 1
- 208000002177 Cataract Diseases 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102400000739 Corticotropin Human genes 0.000 description 1
- 101800000414 Corticotropin Proteins 0.000 description 1
- 244000241257 Cucumis melo Species 0.000 description 1
- 235000015510 Cucumis melo subsp melo Nutrition 0.000 description 1
- RXVWSYJTUUKTEA-UHFFFAOYSA-N D-maltotriose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(O)C(CO)O1 RXVWSYJTUUKTEA-UHFFFAOYSA-N 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000187432 Streptomyces coelicolor Species 0.000 description 1
- 101100154903 Streptomyces glaucescens melC2 gene Proteins 0.000 description 1
- 241000187391 Streptomyces hygroscopicus Species 0.000 description 1
- 241000187412 Streptomyces plicatus Species 0.000 description 1
- 101000895926 Streptomyces plicatus Endo-beta-N-acetylglucosaminidase H Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 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 1
- NSFFHOGKXHRQEW-UHFFFAOYSA-N Thiostrepton B Natural products N1C(=O)C(C)NC(=O)C(=C)NC(=O)C(C)NC(=O)C(C(C)CC)NC(C(C2=N3)O)C=CC2=C(C(C)O)C=C3C(=O)OC(C)C(C=2SC=C(N=2)C2N=3)NC(=O)C(N=4)=CSC=4C(C(C)(O)C(C)O)NC(=O)C(N=4)CSC=4C(=CC)NC(=O)C(C(C)O)NC(=O)C(N=4)=CSC=4C21CCC=3C1=NC(C(=O)NC(=C)C(=O)NC(=C)C(N)=O)=CS1 NSFFHOGKXHRQEW-UHFFFAOYSA-N 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- FJJCIZWZNKZHII-UHFFFAOYSA-N [4,6-bis(cyanoamino)-1,3,5-triazin-2-yl]cyanamide Chemical compound N#CNC1=NC(NC#N)=NC(NC#N)=N1 FJJCIZWZNKZHII-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000023445 activated T cell autonomous cell death Effects 0.000 description 1
- 230000004913 activation Effects 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
- 150000001413 amino acids Chemical group 0.000 description 1
- -1 amino glycol fatty acid Chemical class 0.000 description 1
- 229940126575 aminoglycoside Drugs 0.000 description 1
- 102000006646 aminoglycoside phosphotransferase Human genes 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 229960000182 blood factors Drugs 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 1
- 229960000258 corticotropin Drugs 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 101150077745 ex gene Proteins 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 238000012252 genetic analysis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- FYGDTMLNYKFZSV-UHFFFAOYSA-N mannotriose Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(O)C(O)C2O)CO)C(O)C1O FYGDTMLNYKFZSV-UHFFFAOYSA-N 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000005192 partition Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229930188070 thiostrepton Natural products 0.000 description 1
- NSFFHOGKXHRQEW-AIHSUZKVSA-N thiostrepton Chemical compound C([C@]12C=3SC=C(N=3)C(=O)N[C@H](C(=O)NC(/C=3SC[C@@H](N=3)C(=O)N[C@H](C=3SC=C(N=3)C(=O)N[C@H](C=3SC=C(N=3)[C@H]1N=1)[C@@H](C)OC(=O)C3=CC(=C4C=C[C@H]([C@@H](C4=N3)O)N[C@H](C(N[C@@H](C)C(=O)NC(=C)C(=O)N[C@@H](C)C(=O)N2)=O)[C@@H](C)CC)[C@H](C)O)[C@](C)(O)[C@@H](C)O)=C\C)[C@@H](C)O)CC=1C1=NC(C(=O)NC(=C)C(=O)NC(=C)C(N)=O)=CS1 NSFFHOGKXHRQEW-AIHSUZKVSA-N 0.000 description 1
- 229940063214 thiostrepton Drugs 0.000 description 1
- NSFFHOGKXHRQEW-OFMUQYBVSA-N thiostrepton A Natural products CC[C@H](C)[C@@H]1N[C@@H]2C=Cc3c(cc(nc3[C@H]2O)C(=O)O[C@H](C)[C@@H]4NC(=O)c5csc(n5)[C@@H](NC(=O)[C@H]6CSC(=N6)C(=CC)NC(=O)[C@@H](NC(=O)c7csc(n7)[C@]8(CCC(=N[C@@H]8c9csc4n9)c%10nc(cs%10)C(=O)NC(=C)C(=O)NC(=C)C(=O)N)NC(=O)[C@H](C)NC(=O)C(=C)NC(=O)[C@H](C)NC1=O)[C@@H](C)O)[C@](C)(O)[C@@H](C)O)[C@H](C)O NSFFHOGKXHRQEW-OFMUQYBVSA-N 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- FYGDTMLNYKFZSV-BYLHFPJWSA-N β-1,4-galactotrioside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@H](CO)O[C@@H](O[C@@H]2[C@@H](O[C@@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-BYLHFPJWSA-N 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/001—Oxidoreductases (1.) acting on the CH-CH group of donors (1.3)
-
- 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
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/76—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Actinomyces; for Streptomyces
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y113/00—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13)
- C12Y113/11—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13) with incorporation of two atoms of oxygen (1.13.11)
- C12Y113/11001—Catechol 1,2-dioxygenase (1.13.11.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y113/00—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13)
- C12Y113/11—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13) with incorporation of two atoms of oxygen (1.13.11)
- C12Y113/11002—Catechol 2,3-dioxygenase (1.13.11.2)
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Fodder In General (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Dental Preparations (AREA)
- Enzymes And Modification Thereof (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Transition And Organic Metals Composition Catalysts For Addition Polymerization (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Hydrogenated Pyridines (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ES9102765 | 1991-12-12 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| LTIP237A LTIP237A (en) | 1994-07-15 |
| LT3133B true LT3133B (en) | 1995-01-31 |
Family
ID=8274462
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| LTIP237A LT3133B (en) | 1991-12-12 | 1992-12-11 | Po438, a new calcium-regulated promotor |
Country Status (15)
| Country | Link |
|---|---|
| US (2) | US5385841A (de) |
| EP (1) | EP0546833B1 (de) |
| JP (1) | JP3340164B2 (de) |
| AT (1) | ATE154392T1 (de) |
| AU (1) | AU661073B2 (de) |
| CA (1) | CA2084351C (de) |
| DE (1) | DE69220336T2 (de) |
| DK (1) | DK0546833T3 (de) |
| ES (1) | ES2103902T3 (de) |
| GR (1) | GR3024625T3 (de) |
| IL (1) | IL103975A (de) |
| LT (1) | LT3133B (de) |
| LV (1) | LV10728B (de) |
| RU (1) | RU2112802C1 (de) |
| ZA (1) | ZA929284B (de) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ZA929284B (en) * | 1991-12-12 | 1993-06-02 | Serono Lab | P0438, an new calcium-regulated promoter. |
| US6381353B1 (en) | 1996-08-30 | 2002-04-30 | Marvin Weiss | System for counting colonies of micro-organisms in petri dishes and other culture media |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0148552A1 (de) | 1983-06-07 | 1985-07-17 | Biogen, Inc. | Streptomyces-Expressionssequenz und Methoden zur Expression von DNA-Sequenzen in Streptomyces |
| WO1988007079A1 (en) | 1987-03-09 | 1988-09-22 | Cetus Corporation | Expression of heterologous genes in streptomyces species |
| WO1990014426A2 (en) | 1989-05-19 | 1990-11-29 | Applied Research Systems Ars Holding N.V. | Saf polypeptide, gene, promoter and use for expression in streptomyces |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4766066A (en) * | 1984-09-27 | 1988-08-23 | Eli Lilly And Company | Method of using bacteriophage lambda p1 promoter to produce a functional polypeptide in streptomyces |
| US4745056A (en) * | 1984-10-23 | 1988-05-17 | Biotechnica International, Inc. | Streptomyces secretion vector |
| DE3536182A1 (de) * | 1985-10-10 | 1987-04-16 | Hoechst Ag | Promotor-anordnung fuer streptomyceten-vektoren |
| US5200327A (en) * | 1985-11-06 | 1993-04-06 | Cangene Corporation | Expression system for the secretion of bioactive human granulocyte macrophage colony stimulating factor (GM-CSF) and other heterologous proteins from streptomyces |
| ZA929284B (en) * | 1991-12-12 | 1993-06-02 | Serono Lab | P0438, an new calcium-regulated promoter. |
-
1992
- 1992-11-30 ZA ZA929284A patent/ZA929284B/xx unknown
- 1992-12-02 AU AU29791/92A patent/AU661073B2/en not_active Ceased
- 1992-12-02 CA CA002084351A patent/CA2084351C/en not_active Expired - Fee Related
- 1992-12-04 IL IL10397592A patent/IL103975A/en not_active IP Right Cessation
- 1992-12-09 LV LVP-92-271A patent/LV10728B/en unknown
- 1992-12-10 ES ES92311292T patent/ES2103902T3/es not_active Expired - Lifetime
- 1992-12-10 DE DE69220336T patent/DE69220336T2/de not_active Expired - Fee Related
- 1992-12-10 DK DK92311292.4T patent/DK0546833T3/da active
- 1992-12-10 EP EP92311292A patent/EP0546833B1/de not_active Expired - Lifetime
- 1992-12-10 AT AT92311292T patent/ATE154392T1/de not_active IP Right Cessation
- 1992-12-11 US US07/989,363 patent/US5385841A/en not_active Expired - Lifetime
- 1992-12-11 JP JP33150692A patent/JP3340164B2/ja not_active Expired - Fee Related
- 1992-12-11 RU RU92004585A patent/RU2112802C1/ru not_active IP Right Cessation
- 1992-12-11 LT LTIP237A patent/LT3133B/lt not_active IP Right Cessation
-
1994
- 1994-06-23 US US08/264,526 patent/US5660999A/en not_active Expired - Fee Related
-
1997
- 1997-09-04 GR GR970402263T patent/GR3024625T3/el unknown
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0148552A1 (de) | 1983-06-07 | 1985-07-17 | Biogen, Inc. | Streptomyces-Expressionssequenz und Methoden zur Expression von DNA-Sequenzen in Streptomyces |
| WO1988007079A1 (en) | 1987-03-09 | 1988-09-22 | Cetus Corporation | Expression of heterologous genes in streptomyces species |
| WO1990014426A2 (en) | 1989-05-19 | 1990-11-29 | Applied Research Systems Ars Holding N.V. | Saf polypeptide, gene, promoter and use for expression in streptomyces |
Also Published As
| Publication number | Publication date |
|---|---|
| US5385841A (en) | 1995-01-31 |
| CA2084351C (en) | 2007-04-10 |
| ATE154392T1 (de) | 1997-06-15 |
| RU2112802C1 (ru) | 1998-06-10 |
| JPH05336972A (ja) | 1993-12-21 |
| CA2084351A1 (en) | 1993-06-13 |
| DE69220336T2 (de) | 1997-09-25 |
| AU661073B2 (en) | 1995-07-13 |
| EP0546833A2 (de) | 1993-06-16 |
| LV10728A (lv) | 1995-06-20 |
| ES2103902T3 (es) | 1997-10-01 |
| LTIP237A (en) | 1994-07-15 |
| EP0546833A3 (de) | 1994-04-06 |
| AU2979192A (en) | 1993-06-17 |
| DK0546833T3 (da) | 1997-09-15 |
| ZA929284B (en) | 1993-06-02 |
| DE69220336D1 (de) | 1997-07-17 |
| US5660999A (en) | 1997-08-26 |
| IL103975A0 (en) | 1993-05-13 |
| JP3340164B2 (ja) | 2002-11-05 |
| GR3024625T3 (es) | 1997-12-31 |
| LV10728B (en) | 1995-12-20 |
| EP0546833B1 (de) | 1997-06-11 |
| IL103975A (en) | 1998-08-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4399158B2 (ja) | 乳酸菌における異種遺伝子産物の製造のための改良発酵法 | |
| Nodwell et al. | An oligopeptide permease responsible for the import of an extracellular signal governing aerial mycelium formation in Streptomyces coelicolor | |
| US7083980B2 (en) | Tn5 transposase mutants and the use thereof | |
| Hulett et al. | Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis | |
| van Thor et al. | Salt shock-inducible photosystem I cyclic electron transfer in Synechocystis PCC6803 relies on binding of ferredoxin: NADP+ reductase to the thylakoid membranes via its CpcD phycobilisome-linker homologous N-terminal domain | |
| Errington et al. | Structure and function of the spoIIIJ gene of Bacillus subtilis: a vegetatively expressed gene that is essential for σG activity at an intermediate stage of sporulation | |
| Steiert et al. | A Gene Coding for a Membrane–Bound Hydrolase is Expressed as a Secreted, Soluble Enzyme in Streptomyces Lividans | |
| Donohue et al. | Cloning and expression of the Rhodobacter sphaeroides reaction center H gene | |
| WO2021100640A1 (ja) | 改変シアノバクテリア、改変シアノバクテリアの製造方法、及び、タンパク質の製造方法 | |
| JPS62181789A (ja) | バチルスの制御領域のクロ−ニング及び解析のためのプラスミド | |
| Wang et al. | Bacillus subtilis RNase III gene: cloning, function of the gene in Escherichia coli, and construction of Bacillus subtilis strains with altered rnc loci | |
| Solioz et al. | Operon of vacuolar-type Na (+)-ATPase of Enterococcus hirae | |
| EP0448180B1 (de) | Verfahren zur Modulierung der Produktion von sekundären Metaboliten | |
| EP0429600B1 (de) | Saf-polypeptid, gen, promotor und verwendung für expression in streptomyces | |
| Nesmeyanova et al. | Secretion of the overproduced periplasmic Pho A protein into the medium and accumulation of its precursor in pho A-transformed Escherichia coli strains: involvement of outer membrane vesicles | |
| LT3133B (en) | Po438, a new calcium-regulated promotor | |
| US5389526A (en) | Plasmid vectors for cellular slime moulds of the genus dictyostelium | |
| Casey et al. | Suppression of mutants aberrant in light intensity responses of complementary chromatic adaptation | |
| CA2827774A1 (en) | Regulated gene expression systems and constructs thereof | |
| Mongkolsuk et al. | Transcription termination signal for the cat-86 indicator gene in a Bacillus subtilis promoter-cloning plasmid | |
| RU2114910C1 (ru) | Фрагмент днк, полученный путем молекулярного клонирования из streptomyces griseus атсс 10137, кодирующий saf-полипептид, saf-полипептид, рекомбинантная плазмидная днк, определяющая экспрессию saf-полипептида (варианты), рекомбинантная плазмидная днк pulad3, рекомбинантная плазмидная днк pulad 300, штамм грибов streptomyces lividans, содержащий рекомбинантную плазмидную днк pulad3, и способ экспрессии saf-полипептида | |
| US7718396B2 (en) | Inducible high expression system | |
| JPH05284973A (ja) | 組換プラスミドおよびこれをベクターとして用いる異種蛋白質の分泌生産方法 | |
| RU2221868C2 (ru) | Ген l-аспарагиназы erwinia carotovora и штамм escherichia coli вкпм № в-8174 - продуцент l-аспарагиназы erwinia carotovora | |
| US5656453A (en) | Process for the production of recombinant proteins in streptomycetes |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM9A | Lapsed patents |
Effective date: 20081211 |