DISSOCIATION OF RECA FILAMENTS FROM DUPLEX DNA BY THE RUVA AND RUVB DNA-REPAIR PROTEINS

被引：36

作者：

ADAMS, DE ^{[1
]}

TSANEVA, IR ^{[1
]}

WEST, SC ^{[1
]}

机构：

[1] IMPERIAL CANC RES FUND,CLARE HALL LABS,S MIMMS EN6 3LD,HERTS,ENGLAND

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 21期

关键词：

RECOMBINATION; BRANCH MIGRATION; HELICASE; TOPOISOMERASE; DNA SUPERCOILING;

D O I：

10.1073/pnas.91.21.9901

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The RuvA and RuvB proteins of Escherichia coli act late in recombination and DNA repair to catalyze the branch migration of Holliday junctions made by RecA. In this paper, we show that addition of RuvAB to supercoiled DNA that is bound by RecA leads to the rapid dissociation of the RecA nucleoprotein filament, as determined by a topological assay that measures DNA underwinding and a restriction endonuclease protection assay. Disruption of the RecA filament requires RuvA, RuvB, and hydrolysis of ATP. These findings suggest several important roles for the RuvAB helicase during genetic recombination and DNA repair: (i) displacement of RecA filaments from double-stranded DNA, (ii) interruption of RecA-mediated strand exchange, (iii) RuvAB-catalyzed branch migration, and (iv) recycling of RecA protein.

引用

页码：9901 / 9905

页数：5

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