- それぞれUV修復とSOS修復経路に関与する。これらの遺伝子に変異をもつことにより逆位リピートの組み換えを抑制する。SURE® やSURE® 2株はこの遺伝子を欠損している。(参考1)
参考
- http://www.chem-agilent.com/stratagene/strategies/pdfs/19.2/Strategies%20Vol.2%20No.2_p7.pdf
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/06/11 14:11:13」(JST)
[Wiki en表示]
UvrABC endonuclease is a multienzyme complex in Escherichia coli involved in DNA repair by nucleotide excision repair, and it is, therefore, sometimes called an excinuclease. This UvrABC repair process, sometimes called the short-patch process, involves the removal of twelve nucleotides where a genetic mutation has occurred followed by a DNA polymerase, replacing these aberrant nucleotides with the correct nucleotides and completing the DNA repair. The subunits for this enzyme are encoded in the uvrA, uvrB, and uvrC genes. This enzyme complex is able to repair many different types of damage, including cyclobutyl dimer formation.
Mechanism
- Two UvrA proteins form a dimer and they both have ATPase/GTPase activity.
- The UvrA dimer binds with UvrB and forms a trimer that is able to detect DNA damage.The UvrA dimer functions as the unit responsible for the detection of DNA damage, probably through a mechanism of detecting distortions in the DNA double helix.
- The UvrB part of the trimer attaches to the double helix at the damaged site.
- The UvrA dimer leaves and a UvrC protein comes in and binds to the UvrB monomer and, hence, forms a new UvrBC dimer.
- This dimer is responsible for cleaving the nucleotides either side of the DNA damage. UvrB cleaves a phosphodiester bond four nucleotides downstream of the DNA damage, and the UvrC cleaves a phosphodiester bond eight nucleotides upstream of the DNA damage and created twelve nucleotide excised segment.
- DNA helicase II (sometimes called UvrD) then comes in and removes the excised segment by removing the base pairing. The UvrB still remains in place even though UvrC has disassociated at this stage, as UvrB may be involved to prevent the reannealing of the excised DNA.
- DNA polymerase I comes in and fills in the correct nucleotides sequence, kicking off UvrB in the process, and the last phosphodiester bond is completed by DNA ligase.
See also
- DNA repair
- endonuclease
- Nucleotide excision repair
- DNA
External links
- uvrABC endonuclease at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: esterases (EC 3.1)
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3.1.1: Carboxylic
ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
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3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
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3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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|
3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
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Exoribonuclease |
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3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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English Journal
- An underlying mechanism for the increased mutagenesis of lagging-strand genes in Bacillus subtilis.
- Million-Weaver S1, Samadpour AN1, Moreno-Habel DA1, Nugent P1, Brittnacher MJ1, Weiss E1, Hayden HS1, Miller SI1, Liachko I2, Merrikh H3.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Feb 23. pii: 201416651. [Epub ahead of print]
- We previously reported that lagging-strand genes accumulate mutations faster than those encoded on the leading strand in Bacillus subtilis. Although we proposed that orientation-specific encounters between replication and transcription underlie this phenomenon, the mechanism leading to the increased
- PMID 25713353
- Multilocus sequence typing of a dairy-associated Leuconostoc mesenteroides population reveals clonal structure with intragenic homologous recombination.
- Zhang W1, Liu W1, Song Y1, Xu H1, Menghe B1, Zhang H1, Sun Z2.
- Journal of dairy science.J Dairy Sci.2015 Feb 11. pii: S0022-0302(15)00105-8. doi: 10.3168/jds.2014-9227. [Epub ahead of print]
- Leuconostoc mesenteroides strains play an important role in food fermentation. In this study, 136 strains from different dairy products in China and Mongolia were examined by multilocus sequence typing of 9 housekeeping genes. In total, 82 polymorphic sites were detected among the 9 loci. The number
- PMID 25682150
- Investigation of bacterial nucleotide excision repair using single-molecule techniques.
- Van Houten B1, Kad N2.
- DNA repair.DNA Repair (Amst).2014 Aug;20:41-8. doi: 10.1016/j.dnarep.2013.10.012. Epub 2014 Jan 25.
- Despite three decades of biochemical and structural analysis of the prokaryotic nucleotide excision repair (NER) system, many intriguing questions remain with regard to how the UvrA, UvrB, and UvrC proteins detect, verify and remove a wide range of DNA lesions. Single-molecule techniques have begun
- PMID 24472181
Japanese Journal
- UvrA and UvrB enhance mutations induced by oxidized deoxyribonucleotides
- The gacA Gene of Pseudomonas aeruginosa PAO1 Is Not Required for Full Virulence in Bombyx mori
- Journal of Insect Biotechnology and Sericology 76(2), 2_89-2_95, 2007
- NAID 130004935563
- Crystal Structure of Thermus thermophilus HB8 UvrB Protein, a Key Enzyme of Nucleotide Excision Repair.
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Related Pictures
★リンクテーブル★
[★]
- 関
- 大腸菌
- e14– (McrA–) △(mcrCB-hsdSMR-mrr)171 endA1 supE44 thi-1 gyrA96 relA1 lac recB recJ sbcC umuC::Tn5 (Kanr) uvrC [F'proAB lacIqZ△M15 Tn10 (Tetr)]
特徴
- 不安定なDNAのクローニングでも成功に導くコンピテントセル
- 逆位リピートやZ-DNAを含むDNAの安定性を向上
- 高品質ミニプレップDNAを生産
- F' エピソームを含み、一本鎖DNA レスキューや青/白スクリーニングが可能
参考
- http://www.chem-agilent.com/contents.php?id=300473