STRUCTURAL-ANALYSIS OF THE RUVC-HOLLIDAY JUNCTION COMPLEX REVEALS AN UNFOLDED JUNCTION

被引：106

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：

JOURNAL OF MOLECULAR BIOLOGY | 1995年 / 252卷 / 02期

关键词：

HOLLIDAY JUNCTION; RECOMBINATION; PROTEIN-DNA INTERACTIONS; RESOLVASE; DNA STRUCTURE;

D O I：

10.1006/jmbi.1995.0489

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 RuvC protein of Escherichia coli is an endonuclease that specifically recognises and cleaves Holliday junctions during genetic recombination. The structure of the RuvC-Holliday junction complex has been investigated by DNAse I footprinting and by gel electrophoretic analysis. We find that RuvC binds to the Holliday junction to form a complex that exhibits 2-fold symmetry and in which the three-dimensional structure of the Holliday junction is altered to an unfolded form. This structure is observed in the absence or presence of divalent metal ions and differs from either the unfolded square or the folded stacked X-structures that have been observed with protein-free Holliday junctions. KMnO4 was used to probe the junction DNA upon binding by RuvC, and indicates that base-pairing at the crossover is disrupted within the RuvC-Holliday junction. (C) 1995 Academic Press Limited

引用

页码：213 / 226

页数：14

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