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Originally published In Press as doi:10.1074/jbc.M107945200 on September 10, 2001

J. Biol. Chem., Vol. 276, Issue 45, 41938-41944, November 9, 2001
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Action of RuvAB at Replication Fork Structures*

Peter McGlynnDagger and Robert G. Lloyd§

From the Institute of Genetics, University of Nottingham, Queen's Medical Center, Nottingham, NG7 2UH, United Kingdom

The replicative apparatus often encounters blocks to its progression that necessitate removal of the block and reloading of the replication machinery. In Escherichia coli, a major pathway of replication restart involves unwinding of the stalled fork to generate a four-stranded Holliday junction, which can then be cleaved by the RuvABC helicase-endonuclease. This fork regression may be catalyzed by RecG but is thought to occur even in its absence. Here we test whether RuvAB helicase can also catalyze the unwinding of forked DNA to form Holliday junctions. We find that fork DNA is unwound in the direction required for Holliday junction formation only if the loading of RuvB is restricted to the parental duplex DNA arm. If the binding of RuvB is unrestricted, then RuvAB preferentially unwinds forks in the opposite direction. This is probably related to the greater efficiency of two opposed RuvB hexamers operating across a junction compared with a single hexamer. These data argue against RuvAB acting directly at damaged replication forks and imply that other mechanisms must operate in vivo to catalyze Holliday junction formation.

* This work was supported by a program grant from the Medical Research Council (to R. G. L. and Gary Sharples).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of the Lister Institute-Jenner Research Fellowship.

§ To whom correspondence should be addressed. Tel.: 44-115-9709406; Fax: 44-115-9709906; E-mail: bob.lloyd@nottingham.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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