Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the Holliday junction

被引：21

作者：

Rafferty, JB

Ingleston, SM

Hargreaves, D

Artymiuk, PJ

Sharples, GJ

Lloyd, RG

Rice, DW ^{[1
]}

机构：

[1] Univ Sheffield, Western Bank, Krebs Inst, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England

[2] Univ Nottingham, Queens Med Ctr, Dept Genet, Nottingham NG7 2UH, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1998年 / 278卷 / 01期

基金：

英国惠康基金;

关键词：

DNA polymerase; Holliday junction; homologous recombination; RuvA; structural similarities;

D O I：

10.1006/jmbi.1998.1697

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：

Comparison of the structure of Escherichia coli RuvA with other proteins in the Protein Data Bank gives insights into the probable modes of association of RuvA with the Hollday junction during homologous recombination. All three domains of the RuvA protein possess striking structural similarities to other DNA-binding proteins. Additionally, the second domain of RuvA contains two copies of the helix-hairpin-helix (HhH) structural motif, which has been implicated in non-sequence-specific DNA binding. The two copies of the motif are related by approximate 2-fold symmetry and may form a bidentate DNA-binding module. The results described provide support for the organization of the arms of the DNA in our RuvA/Holliday junction complex model and support the involvement of the HhH motifs in DNA binding. (C) 1998 Academic Press Limited.

引用

页码：105 / 116

页数：12

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