A RecA filament capping mechanism for RecX protein

被引：96

作者：

Drees, JC ^{[1
]}

Lusetti, SL ^{[1
]}

Chitteni-Pattu, S ^{[1
]}

Inman, RB ^{[1
]}

Cox, MM ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA

来源：

MOLECULAR CELL | 2004年 / 15卷 / 05期

关键词：

D O I：

10.1016/j.molcel.2004.08.026

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The RecX protein is a potent inhibitor of RecA protein activities. RecX functions by specifically blocking the extension of RecA filaments. In vitro, this leads to a net disassembly of RecA protein from circular single-stranded DNA. Based on multiple observations, we propose that RecX has a RecA filament capping activity. This activity has predictable effects on the formation and disassembly of RecA filaments. In vivo, the RecX protein may limit the length of RecA filaments formed during recombinational DNA repair and other activities. RecX protein interacts directly with RecA protein, but appears to interact in a functionally significant manner only with RecA filaments bound to DNA.

引用

页码：789 / 798

页数：10

共 52 条

[1] Quantitative analysis of the kinetics of end-dependent disassembly of RecA filaments from ssDNA [J].