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关于“奇”在细菌重组中作用的新旧概念

Old and new concepts for the role of chi in bacterial recombination.

作者信息

Stahl F, Myers R

机构信息

Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.

出版信息

J Hered. 1995 Sep-Oct;86(5):327-9. doi: 10.1093/oxfordjournals.jhered.a111599.

DOI:10.1093/oxfordjournals.jhered.a111599
PMID:7560868
Abstract

The DNA sequence 5'[GCTGGTGG]3', which is called chi, stimulates recombination that is mediated by the RecBCD pathway of Escherichia coli. In 1981, a model was proposed in which the RecBCD enzyme enters DNA at a double-chain end. The enzyme then travels between the chains by unwinding and rewinding the DNA at different rates so that the traveling enzyme becomes encumbered by a region of unwound DNA. Upon meeting chi, the enzyme was supposed to cut one of the two unwound chains, generating thereby a recombinagenic single-chain end. The model, based on microscopical observations of RecBCD enzyme interacting with linear duplex DNA, was supported by the subsequent finding that RecBCD acting in vitro under certain conditions did deliver a nick at chi. This widely embraced model has been challenged by a model in which the exonuclease activity of RecBCD destroys DNA from the enzyme's entry site to chi. The role of chi according to the new model is to inhibit this nuclease activity of RecBCD, perhaps by ejecting the RecD subunit from the enzyme, thereby revealing the enzyme's recombinase activity.

摘要

被称为χ的DNA序列5'[GCTGGTGG]3'可刺激由大肠杆菌RecBCD途径介导的重组。1981年,有人提出了一个模型,其中RecBCD酶在双链末端进入DNA。然后该酶通过以不同速率解开和重新缠绕DNA在两条链之间移动,使得移动的酶被一段解旋的DNA区域所阻碍。遇到χ时,该酶应该切割两条解旋链中的一条,从而产生一个重组单链末端。该模型基于对RecBCD酶与线性双链DNA相互作用的显微镜观察,随后发现RecBCD在某些条件下在体外确实在χ处产生一个切口,这支持了该模型。这个被广泛接受的模型受到了另一个模型的挑战,在这个模型中,RecBCD的核酸外切酶活性从酶的进入位点到χ破坏DNA。根据新模型,χ的作用是抑制RecBCD的这种核酸酶活性,可能是通过从酶中排出RecD亚基,从而揭示酶的重组酶活性。

相似文献

1
Old and new concepts for the role of chi in bacterial recombination.关于“奇”在细菌重组中作用的新旧概念
J Hered. 1995 Sep-Oct;86(5):327-9. doi: 10.1093/oxfordjournals.jhered.a111599.
2
Chi and the RecBC D enzyme of Escherichia coli.大肠杆菌的Chi序列与RecBC D酶
Annu Rev Genet. 1994;28:49-70. doi: 10.1146/annurev.ge.28.120194.000405.
3
Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot chi in vitro: evidence for functional inactivation or loss of the RecD subunit.体外重组热点chi对大肠杆菌RecBCD酶的可逆失活作用:RecD亚基功能失活或缺失的证据
Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2980-4. doi: 10.1073/pnas.91.8.2980.
4
The recombination hot spot chi activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy.重组热点chi通过将大肠杆菌转变为recD突变体表型模拟物来激活RecBCD重组。
Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6244-8. doi: 10.1073/pnas.92.14.6244.
5
Further tests of a recombination model in which chi removes the RecD subunit from the RecBCD enzyme of Escherichia coli.对一种重组模型的进一步测试,在该模型中,chi从大肠杆菌的RecBCD酶中去除RecD亚基。
Genetics. 1990 Nov;126(3):519-33. doi: 10.1093/genetics/126.3.519.
6
The RecD subunit of the Escherichia coli RecBCD enzyme inhibits RecA loading, homologous recombination, and DNA repair.大肠杆菌RecBCD酶的RecD亚基会抑制RecA装载、同源重组和DNA修复。
Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7399-404. doi: 10.1073/pnas.130192397.
7
The recombination hotspot chi is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme.重组热点chi是一种调控序列,其作用是减弱大肠杆菌RecBCD酶的核酸酶活性。
Cell. 1993 Apr 9;73(1):87-96. doi: 10.1016/0092-8674(93)90162-j.
8
Bacteriophage P22 Abc2 protein binds to RecC increases the 5' strand nicking activity of RecBCD and together with lambda bet, promotes Chi-independent recombination.噬菌体P22 Abc2蛋白与RecC结合,增强RecBCD的5'链切口活性,并与λ bet一起促进不依赖于Chi序列的重组。
J Mol Biol. 2000 Feb 18;296(2):385-401. doi: 10.1006/jmbi.1999.3486.
9
The hybrid recombinational repair pathway operates in a χ activity deficient recC1004 mutant of Escherichia coli.大肠杆菌 recC1004 突变体中,杂合重组修复途径在 χ 活性缺失的情况下起作用。
Biochimie. 2012 Sep;94(9):1918-25. doi: 10.1016/j.biochi.2012.05.008. Epub 2012 May 19.
10
Chi-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules.单个RecBCD解旋酶/核酸酶分子对Chi序列的识别与DNA转位
Nature. 2001 Jan 18;409(6818):370-4. doi: 10.1038/35053124.

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