Active displacement of RecA filaments by UvrD translocase activity

被引:45
作者
Petrova, Vessela [1 ]
Chen, Stefanie H. [2 ]
Molzberger, Eileen T. [2 ]
Tomko, Eric [3 ]
Chitteni-Pattu, Sindhu [2 ]
Jia, Haifeng [3 ]
Ordabayev, Yerdos [3 ]
Lohman, Timothy M. [3 ]
Cox, Michael M. [1 ,2 ]
机构
[1] Univ Wisconsin, Program Cellular & Mol Biol, Madison, WI 53706 USA
[2] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA
[3] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA
关键词
SINGLE-STRANDED-DNA; ESCHERICHIA-COLI-UVRD; STALLED REPLICATION FORKS; NICKED CIRCULAR DNA; HELICASE-II; ATP HYDROLYSIS; BINDING-PROTEIN; C-TERMINUS; IN-VITRO; E; COLI;
D O I
10.1093/nar/gkv186
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 UvrD helicase has been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro. We demonstrate that UvrD utilizes an active mechanism to remove RecA from the DNA. Efficient RecA removal depends on the availability of DNA binding sites for UvrD and/or the accessibility of the RecA filament ends. The removal of RecA from DNA also requires ATP hydrolysis by the UvrD helicase but not by RecA protein. The RecA-removal activity of UvrD is slowed by RecA variants with enhanced DNA-binding properties. The ATPase rate of UvrD during RecA removal is much slower than the ATPase activity of UvrD when it is functioning either as a translocase or a helicase on DNA in the absence of RecA. Thus, in this context UvrD may operate in a specialized disassembly mode.
引用
收藏
页码:4133 / 4149
页数:17
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