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

被引:55
作者
Drees, JC [1 ]
Lusetti, SL [1 ]
Cox, MM [1 ]
机构
[1] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA
关键词
D O I
10.1074/jbc.M409050200
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 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 Mg2+ 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.
引用
收藏
页码:52991 / 52997
页数:7
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