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大肠杆菌RecX蛋白对RecA蛋白的抑制作用:受RecA蛋白C末端和丝状功能状态的调节

Inhibition of RecA protein by the Escherichia coli RecX protein: modulation by the RecA C terminus and filament functional state.

作者信息

Drees Julia C, Lusetti Shelley L, Cox Michael M

机构信息

Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Dr., Madison, WI 53706-1544, USA.

出版信息

J Biol Chem. 2004 Dec 17;279(51):52991-7. doi: 10.1074/jbc.M409050200. Epub 2004 Oct 4.

DOI:10.1074/jbc.M409050200
PMID:15466870
Abstract

The RecX protein is a potent inhibitor of RecA activities. We identified several factors that affect RecX-RecA interaction. The interaction is enhanced by the RecA C terminus and by significant concentrations of free Mg(2+) ion. The interaction is also enhanced by an N-terminal His(6) tag on the RecX protein. We conclude that RecX protein interacts most effectively with a RecA functional state designated A(o) and that the RecA C terminus has a role in modulating the interaction. We further identified a C-terminal point mutation in RecA protein (E343K) that significantly alters the interaction between RecA and RecX proteins.

摘要

RecX蛋白是RecA活性的有效抑制剂。我们鉴定出了几种影响RecX-RecA相互作用的因素。RecA的C末端以及高浓度的游离Mg(2+)离子可增强这种相互作用。RecX蛋白上的N末端His(6)标签也可增强这种相互作用。我们得出结论,RecX蛋白与一种称为A(o)的RecA功能状态相互作用最为有效,且RecA的C末端在调节这种相互作用中发挥作用。我们进一步鉴定出RecA蛋白中的一个C末端点突变(E343K),该突变显著改变了RecA与RecX蛋白之间的相互作用。

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Inhibition of RecA protein by the Escherichia coli RecX protein: modulation by the RecA C terminus and filament functional state.大肠杆菌RecX蛋白对RecA蛋白的抑制作用:受RecA蛋白C末端和丝状功能状态的调节
J Biol Chem. 2004 Dec 17;279(51):52991-7. doi: 10.1074/jbc.M409050200. Epub 2004 Oct 4.
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