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全局调控因子H-NS直接作用于转座体以促进Tn10转座。

The global regulator H-NS acts directly on the transpososome to promote Tn10 transposition.

作者信息

Wardle Simon J, O'Carroll Michelle, Derbyshire Keith M, Haniford David B

机构信息

Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1 Canada.

出版信息

Genes Dev. 2005 Sep 15;19(18):2224-35. doi: 10.1101/gad.1338905.

DOI:10.1101/gad.1338905
PMID:16166383
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1221892/
Abstract

The histone-like nucleoid structuring (H-NS) protein is a global transcriptional regulator that is known to regulate stress response pathways and virulence genes in bacteria. It has also been implicated in the regulation of bacterial transposition systems, including Tn10. We demonstrate here that H-NS promotes Tn10 transposition by binding directly to the transposition complex (or transpososome). We present evidence that, upon binding, H-NS induces the unfolding of the Tn10 transpososome and helps to maintain the transpososome in an unfolded state. This ensures that intermolecular (as opposed to self-destructive intramolecular) transposition events are favored. We present evidence that H-NS binding to the flanking donor DNA of the transpososome is the initiating event in the unfolding process. We propose that by recruiting H-NS as a modulator of transposition, Tn10 has evolved a means of sensing changes in host physiology, as the amount of H-NS in the cell, as well its activity, are responsive to changes in environmental conditions. Sensing of environmental changes through H-NS would allow transposition to occur when it is most opportune for both the transposon and the host.

摘要

类组蛋白核仁结构蛋白(H-NS)是一种全局性转录调节因子,已知其可调节细菌中的应激反应途径和毒力基因。它还与细菌转座系统(包括Tn10)的调节有关。我们在此证明,H-NS通过直接结合转座复合物(或转座体)来促进Tn10转座。我们提供的证据表明,结合后,H-NS会诱导Tn10转座体展开,并有助于将转座体维持在展开状态。这确保了分子间(而非自我破坏的分子内)转座事件占优势。我们提供的证据表明,H-NS与转座体侧翼供体DNA的结合是展开过程中的起始事件。我们提出,通过招募H-NS作为转座的调节剂,Tn10已经进化出一种感知宿主生理变化的方式,因为细胞中H-NS的量及其活性会对环境条件的变化做出反应。通过H-NS感知环境变化将使转座在对转座子和宿主最有利的时机发生。

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Genes Dev. 2005 Sep 15;19(18):2224-35. doi: 10.1101/gad.1338905.
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本文引用的文献

1
Cyclic changes in the affinity of protein-DNA interactions drive the progression and regulate the outcome of the Tn10 transposition reaction.蛋白质与DNA相互作用亲和力的周期性变化驱动了Tn10转座反应的进程并调控其结果。
Nucleic Acids Res. 2005 Apr 6;33(6):1982-92. doi: 10.1093/nar/gki348. Print 2005.
2
Translational control of tetracycline resistance and conjugation in the Bacteroides conjugative transposon CTnDOT.拟杆菌属接合转座子CTnDOT中四环素抗性和接合作用的翻译调控
J Bacteriol. 2005 Apr;187(8):2673-80. doi: 10.1128/JB.187.8.2673-2680.2005.
3
Tn10 transposase mutants with altered transpososome unfolding properties are defective in hairpin formation.转座体解折叠特性发生改变的Tn10转座酶突变体在发夹形成方面存在缺陷。
J Mol Biol. 2005 Feb 25;346(3):703-16. doi: 10.1016/j.jmb.2004.12.009. Epub 2005 Jan 18.
4
YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes with H-NS and StpA.YdgT是大肠杆菌中与Hha同源的蛋白,它与H-NS和StpA形成异源复合物。
Mol Microbiol. 2004 Oct;54(1):251-63. doi: 10.1111/j.1365-2958.2004.04268.x.
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Regulation of transposition in bacteria.细菌中转座的调控。
Res Microbiol. 2004 Jun;155(5):387-98. doi: 10.1016/j.resmic.2004.01.008.
6
The effect of host-encoded nucleoid proteins on transposition: H-NS influences targeting of both IS903 and Tn10.宿主编码的类核蛋白对转座的影响:H-NS影响IS903和Tn10的靶向。
Mol Microbiol. 2004 May;52(4):1055-67. doi: 10.1111/j.1365-2958.2004.04051.x.
7
H-NS: a universal regulator for a dynamic genome.H-NS:动态基因组的通用调控因子。
Nat Rev Microbiol. 2004 May;2(5):391-400. doi: 10.1038/nrmicro883.
8
Protective role for H-NS protein in IS1 transposition.H-NS蛋白在IS1转座中的保护作用。
J Bacteriol. 2004 Apr;186(7):2091-8. doi: 10.1128/JB.186.7.2091-2098.2004.
9
DNA looping and catalysis; the IHF-folded arm of Tn10 promotes conformational changes and hairpin resolution.DNA环化与催化;Tn10的IHF折叠臂促进构象变化和发夹结构解析。
Mol Cell. 2004 Feb 27;13(4):537-47. doi: 10.1016/s1097-2765(04)00052-8.
10
The positive and negative regulation of Tn10 transposition by IHF is mediated by structurally asymmetric transposon arms.整合宿主因子(IHF)对Tn10转座的正负调控是由结构不对称的转座子臂介导的。
Nucleic Acids Res. 2003 Oct 15;31(20):5868-76. doi: 10.1093/nar/gkg797.