CA2577180A1 - Single protein production in living cells facilitated by a messenger rna interferase - Google Patents
Single protein production in living cells facilitated by a messenger rna interferase Download PDFInfo
- Publication number
- CA2577180A1 CA2577180A1 CA002577180A CA2577180A CA2577180A1 CA 2577180 A1 CA2577180 A1 CA 2577180A1 CA 002577180 A CA002577180 A CA 002577180A CA 2577180 A CA2577180 A CA 2577180A CA 2577180 A1 CA2577180 A1 CA 2577180A1
- Authority
- CA
- Canada
- Prior art keywords
- mutated
- acid sequence
- nucleic acid
- target protein
- mrna interferase
- 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.)
- Abandoned
Links
- 108020004999 messenger RNA Proteins 0.000 title claims abstract description 125
- 230000014616 translation Effects 0.000 title claims abstract description 41
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 155
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 123
- 230000001413 cellular effect Effects 0.000 claims abstract description 44
- 230000014509 gene expression Effects 0.000 claims abstract description 39
- 238000001243 protein synthesis Methods 0.000 claims abstract description 28
- 241000588724 Escherichia coli Species 0.000 claims abstract description 17
- 108010058643 Fungal Proteins Proteins 0.000 claims abstract description 8
- 108090000144 Human Proteins Proteins 0.000 claims abstract description 4
- 102000003839 Human Proteins Human genes 0.000 claims abstract 3
- 210000004027 cell Anatomy 0.000 claims description 104
- 150000007523 nucleic acids Chemical group 0.000 claims description 101
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 69
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 66
- 229920001184 polypeptide Polymers 0.000 claims description 61
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 61
- 238000000034 method Methods 0.000 claims description 52
- 108020004705 Codon Proteins 0.000 claims description 40
- 230000001939 inductive effect Effects 0.000 claims description 37
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 31
- 239000013604 expression vector Substances 0.000 claims description 29
- 239000003795 chemical substances by application Substances 0.000 claims description 10
- 239000012634 fragment Substances 0.000 claims description 8
- 230000001105 regulatory effect Effects 0.000 claims description 6
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 5
- 229960000643 adenine Drugs 0.000 claims description 4
- 230000001965 increasing effect Effects 0.000 claims description 4
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 4
- 231100000331 toxic Toxicity 0.000 claims description 4
- 230000002588 toxic effect Effects 0.000 claims description 4
- 210000004962 mammalian cell Anatomy 0.000 claims description 3
- 238000003752 polymerase chain reaction Methods 0.000 claims description 3
- 108010077805 Bacterial Proteins Proteins 0.000 claims 2
- 102000008300 Mutant Proteins Human genes 0.000 claims 1
- 108010021466 Mutant Proteins Proteins 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 abstract description 15
- 108010093099 Endoribonucleases Proteins 0.000 abstract description 9
- 108010052285 Membrane Proteins Proteins 0.000 abstract description 8
- 102000018697 Membrane Proteins Human genes 0.000 abstract description 7
- 230000015572 biosynthetic process Effects 0.000 abstract description 7
- 238000003786 synthesis reaction Methods 0.000 abstract description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 abstract description 5
- 238000001727 in vivo Methods 0.000 abstract description 5
- 230000012010 growth Effects 0.000 abstract description 4
- 230000001580 bacterial effect Effects 0.000 abstract description 3
- 230000002103 transcriptional effect Effects 0.000 abstract description 3
- 231100000699 Bacterial toxin Toxicity 0.000 abstract description 2
- 239000000688 bacterial toxin Substances 0.000 abstract description 2
- 238000005516 engineering process Methods 0.000 abstract description 2
- 230000002459 sustained effect Effects 0.000 abstract description 2
- 102100030011 Endoribonuclease Human genes 0.000 abstract 1
- 208000036758 Postinfectious cerebellitis Diseases 0.000 description 65
- 101710139422 Eotaxin Proteins 0.000 description 48
- 102100023688 Eotaxin Human genes 0.000 description 42
- 108020004707 nucleic acids Proteins 0.000 description 29
- 102000039446 nucleic acids Human genes 0.000 description 29
- 150000001413 amino acids Chemical class 0.000 description 24
- 108090000233 Signal peptidase II Proteins 0.000 description 19
- 230000006698 induction Effects 0.000 description 18
- 239000013612 plasmid Substances 0.000 description 17
- 108020004414 DNA Proteins 0.000 description 15
- 230000020800 chemokine (C-C motif) ligand 11 production Effects 0.000 description 13
- 230000000694 effects Effects 0.000 description 13
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 13
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 12
- 101150048352 mazF gene Proteins 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 11
- 238000010348 incorporation Methods 0.000 description 11
- 239000002773 nucleotide Substances 0.000 description 11
- 125000003729 nucleotide group Chemical group 0.000 description 11
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 10
- 125000000539 amino acid group Chemical group 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 239000013598 vector Substances 0.000 description 10
- 102100024341 10 kDa heat shock protein, mitochondrial Human genes 0.000 description 9
- 101710122378 10 kDa heat shock protein, mitochondrial Proteins 0.000 description 9
- 239000012528 membrane Substances 0.000 description 8
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 7
- 238000013518 transcription Methods 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- 239000002609 medium Substances 0.000 description 6
- 238000002741 site-directed mutagenesis Methods 0.000 description 6
- 238000013519 translation Methods 0.000 description 6
- 101100389345 Bacillus subtilis (strain 168) ndoA gene Proteins 0.000 description 5
- 102100030013 Endoribonuclease Human genes 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 230000002068 genetic effect Effects 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000000411 inducer Substances 0.000 description 5
- 210000003705 ribosome Anatomy 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 4
- 101000978392 Homo sapiens Eotaxin Proteins 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 3
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 3
- 102000002494 Endoribonucleases Human genes 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- 108020004566 Transfer RNA Proteins 0.000 description 3
- 230000037429 base substitution Effects 0.000 description 3
- 230000003915 cell function Effects 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 210000000349 chromosome Anatomy 0.000 description 3
- 230000037149 energy metabolism Effects 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 230000035479 physiological effects, processes and functions Effects 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 108020003589 5' Untranslated Regions Proteins 0.000 description 2
- 238000011537 Coomassie blue staining Methods 0.000 description 2
- -1 CspA (Qing et al Proteins 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 206010012335 Dependence Diseases 0.000 description 2
- 108091092195 Intron Proteins 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 230000006819 RNA synthesis Effects 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000001851 biosynthetic effect Effects 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 230000002708 enhancing effect Effects 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 239000006481 glucose medium Substances 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 108020004418 ribosomal RNA Proteins 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 108700012359 toxins Proteins 0.000 description 2
- 108010087967 type I signal peptidase Proteins 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 230000035899 viability Effects 0.000 description 2
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- 230000002407 ATP formation Effects 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010049152 Cold Shock Proteins and Peptides Proteins 0.000 description 1
- 101710090243 Cold shock protein CspB Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 241000701867 Enterobacteria phage T7 Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- AYIZHKDZYOSOGY-IUCAKERBSA-N His-Met Chemical group CSCC[C@@H](C([O-])=O)NC(=O)[C@@H]([NH3+])CC1=CN=CN1 AYIZHKDZYOSOGY-IUCAKERBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108010054278 Lac Repressors Proteins 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
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
- 101710092121 Major cold shock protein Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108020005196 Mitochondrial DNA Proteins 0.000 description 1
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
- 108010078762 Protein Precursors Proteins 0.000 description 1
- 102000014961 Protein Precursors Human genes 0.000 description 1
- 230000004570 RNA-binding Effects 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108010034634 Repressor Proteins Proteins 0.000 description 1
- 102000009661 Repressor Proteins Human genes 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000002278 Ribosomal Proteins Human genes 0.000 description 1
- 108010000605 Ribosomal Proteins Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000001147 anti-toxic effect Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000027455 binding Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000001486 biosynthesis of amino acids Effects 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 230000004637 cellular stress Effects 0.000 description 1
- 239000005482 chemotactic factor Substances 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 230000001332 colony forming effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 101150110403 cspA gene Proteins 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 230000002542 deteriorative effect Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 230000005059 dormancy Effects 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002327 eosinophilic effect Effects 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 210000002706 plastid Anatomy 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/22—Ribonucleases RNAses, DNAses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Cell Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US62497604P | 2004-11-04 | 2004-11-04 | |
US60/624,976 | 2004-11-04 | ||
PCT/US2005/040107 WO2006055292A2 (en) | 2004-11-04 | 2005-11-04 | Single protein production in living cells facilitated by a messenger rna interferase |
Publications (1)
Publication Number | Publication Date |
---|---|
CA2577180A1 true CA2577180A1 (en) | 2006-05-26 |
Family
ID=36407606
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA002577180A Abandoned CA2577180A1 (en) | 2004-11-04 | 2005-11-04 | Single protein production in living cells facilitated by a messenger rna interferase |
Country Status (6)
Country | Link |
---|---|
EP (1) | EP1812582A4 (ja) |
JP (1) | JP5013375B2 (ja) |
KR (1) | KR101064783B1 (ja) |
CN (1) | CN101052713B (ja) |
CA (1) | CA2577180A1 (ja) |
WO (1) | WO2006055292A2 (ja) |
Families Citing this family (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2007020873A1 (ja) * | 2005-08-16 | 2007-02-22 | Takara Bio Inc. | 免疫不全ウイルス感染症の治療または予防のための核酸 |
WO2010040134A2 (en) | 2008-10-04 | 2010-04-08 | University Of Medicine And Dentistry Of New Jersey | Independently inducible system of gene expression |
EP2848695A1 (en) * | 2013-09-16 | 2015-03-18 | Inria Institut National de Recherche en Informatique et en Automatique | Method for producing metabolites, peptides and recombinant proteins |
CN103484471B (zh) * | 2013-09-30 | 2015-07-08 | 王悦 | 人表皮细胞生长因子核酸序列及大肠杆菌表达载体 |
KR101776368B1 (ko) * | 2014-10-02 | 2017-09-07 | 서울시립대학교 산학협력단 | 전령 rna 나노입자 및 그 제조방법 |
TW202000240A (zh) * | 2018-02-23 | 2020-01-01 | 日商盧卡科學股份有限公司 | 用於在粒線體內使蛋白質表現之核酸、封入前述核酸之脂質膜結構體及其等之用途 |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5807718A (en) * | 1994-12-02 | 1998-09-15 | The Scripps Research Institute | Enzymatic DNA molecules |
EP2298869A1 (en) * | 2003-06-13 | 2011-03-23 | University Of Medicine And Dentistry Of New Jersey | Recombinant protein production in the presence of mRNA interferase |
-
2005
- 2005-11-04 KR KR1020077012576A patent/KR101064783B1/ko not_active IP Right Cessation
- 2005-11-04 JP JP2007540092A patent/JP5013375B2/ja not_active Expired - Fee Related
- 2005-11-04 CA CA002577180A patent/CA2577180A1/en not_active Abandoned
- 2005-11-04 CN CN2005800323789A patent/CN101052713B/zh not_active Expired - Fee Related
- 2005-11-04 EP EP05851377A patent/EP1812582A4/en not_active Withdrawn
- 2005-11-04 WO PCT/US2005/040107 patent/WO2006055292A2/en active Application Filing
Also Published As
Publication number | Publication date |
---|---|
KR101064783B1 (ko) | 2011-09-14 |
KR20080088350A (ko) | 2008-10-02 |
CN101052713A (zh) | 2007-10-10 |
WO2006055292A3 (en) | 2006-08-03 |
JP5013375B2 (ja) | 2012-08-29 |
CN101052713B (zh) | 2011-01-26 |
WO2006055292A2 (en) | 2006-05-26 |
EP1812582A2 (en) | 2007-08-01 |
JP2008518623A (ja) | 2008-06-05 |
EP1812582A4 (en) | 2013-03-20 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP7308160B2 (ja) | メチロトローフ酵母の遺伝子操作の発現構築物および方法 | |
US11427932B2 (en) | Materials and methods for protein production | |
WO2007137144A2 (en) | Single protein production in living cells facilitated by a messenger rna interferase | |
CA2577180A1 (en) | Single protein production in living cells facilitated by a messenger rna interferase | |
CN113564171B (zh) | 一种提高多肽可溶性表达产量的方法 | |
US7985575B2 (en) | Single protein production in living cells facilitated by a messenger RNA interferase | |
Linova et al. | A novel approach for production of an active N-terminally truncated Ulp1 (SUMO protease 1) catalytic domain from Escherichia coli inclusion bodies | |
JP4857260B2 (ja) | 低温性微生物由来エンドヌクレアーゼ | |
Chandler et al. | At UBP3 and At UBP4 are two closely related Arabidopsis thaliana ubiquitin-specific proteases present in the nucleus | |
Hennessy et al. | Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium tumefaciens identifies amino acid residues critical to its in vivo function | |
Klanner et al. | MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa | |
JP6991423B2 (ja) | グルコースオキシダーゼCnGODA及びその遺伝子ならびに使用 | |
JP3549210B2 (ja) | プラスミド | |
CN110951711B (zh) | 一种具有降解手性酯活性的酯酶及其编码基因和应用 | |
JP5240970B2 (ja) | 界面活性剤存在下で安定なコレステロールオキシダーゼ | |
US20090259035A1 (en) | Method for producing recombinant RNase A | |
JP4714848B2 (ja) | Dnaポリメラーゼ変異体 | |
JPWO2007010740A1 (ja) | 新規なエンドリボヌクレアーゼ | |
JP2001103972A (ja) | ルシフェリンを再生する能力を有するタンパク質をコードする遺伝子、新規な組み換え体dna及びルシフェリンを再生する能力を有するタンパク質の製造法 | |
Kim | A microbial D-hydantoinase is stabilized and overexpressed as a catalytically active dimer by truncation and insertion of the C-terminal region | |
WO2023096513A1 (en) | Tritirachium album proteinase k mutant and its zymogen, expression plasmid, recombinant pichia pastoris strain and method of producing the mature form of proteinase k mutant | |
CA2594178C (en) | Methods of production of modified proteins | |
JP2001161375A (ja) | コレステロール・エステラーゼ遺伝子、組み換え体dna及びコレステロール・エステラーゼの製造法 | |
JP2002247985A (ja) | Dna修復酵素遺伝子 | |
WO2005023854A2 (en) | Modified 6-phosphofructo-1-kinase of the fungus aspergillus niger |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
EEER | Examination request | ||
FZDE | Discontinued |