RUVC PROTEIN RESOLVES HOLLIDAY JUNCTIONS VIA CLEAVAGE OF THE CONTINUOUS (NONCROSSOVER) STRANDS

被引：69

作者：

BENNETT, RJ ^{[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 | 1995年 / 92卷 / 12期

关键词：

RECOMBINATION; DNA REPAIR; RESOLVE; STACKED X-STRUCTURE; HYDROXYL RADICAL FOOTPRINTING;

D O I：

10.1073/pnas.92.12.5635

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 RuvC protein of Escherichia coli resolves Holliday junctions during genetic recombination and the postreplicational repair of DNA damage, Using synthetic Holliday junctions that are constrained to adopt defined isomeric configurations, we show that resolution occurs by symmetric cleavage of the continuous (noncrossing) pair of DNA strands. This result contrasts with that observed with phage T4 endonuclease VII, which cleaves the pair of crossing strands. In the presence of RuvC, the pair of continuous strands (i.e., the target strands for cleavage) exhibit a hypersensitivity to hydroxyl radicals, These results indicate that the continuous strands are distorted within the RuvC/Holliday junction complex and that RuvC-mediated resolution events require protein-directed structural changes to the four-way junction.

引用

页码：5635 / 5639

页数：5

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