Helicase-defective RuvBD113E promotes RuvAB-mediated branch migration in vitro

被引：9

作者：

George, H

Mézard, C

Stasiak, A

West, SC ^{[1
]}

机构：

[1] Imperial Canc Res Fund, Clare Hall Labs, Genet Recombinat Lab, S Mimms EN6 3LD, Herts, England

[2] Univ Lausanne, Lab Anal Ultrastruct, CH-1015 Lausanne, Switzerland

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1999年 / 293卷 / 03期

关键词：

recombination; DNA repair; Holliday junction; ATPase; DNA unwinding;

D O I：

10.1006/jmbi.1999.3187

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：

In Escherichia coli, the RuvA and RuvB proteins interact at Holliday junctions to promote branch migration leading to the formation of heteroduplex DNA. RuvA provides junction-binding specificity and RuvB drives Am-dependent branch migration. Since RuvB contains sequence motifs characteristic of a DNA helicase and RuvAB exhibit helicase activity in vitro, we have analysed the role of DNA unwinding in relation to branch migration. A mutant RuvB protein, RUVBD113E, mutated in helicase motif II (the DExx box), has been purified to homogeneity. The mutant protein forms hexameric;rings on DNA similar to those formed by wild-type protein and promotes branch migration in the presence of RuvA. However, RuvB(D113E) exhibits reduced ATPase activity and is severely compromised in its DNA helicase activity. Models for RuvAB-mediated branch migration that invoke only Limited DNA unwinding activity are proposed. (C) 1999 Academic Press.

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收藏

页码：505 / 519

页数：15

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