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J. Biol. Chem., Vol. 280, Issue 48, 39693-39700, December 2, 2005

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PriB Stimulates PriA Helicase via an Interaction with Single-stranded DNA^*

Chris J. Cadman, Matthew Lopper, Peter B. Moon, James L. Keck, and Peter McGlynn1

From the School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom and the Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison, Wisconsin 53706

The frequency with which replication forks break down in all organisms requires that specific mechanisms ensure completion of genome duplication. In Escherichia coli a major pathway for reloading of the replicative apparatus at sites of fork breakdown is dependent on PriA helicase. PriA acts in conjunction with PriB and DnaT to effect loading of the replicative helicase DnaB back onto the lagging strand template, either at stalled fork structures or at recombination intermediates. Here we showed that PriB stimulates PriA helicase, acting to increase the apparent processivity of PriA. This stimulation correlates with the ability of PriB to form a ternary complex with PriA and DNA structures containing single-stranded DNA, suggesting that the known single-stranded DNA binding function of PriB facilitates unwinding by PriA helicase. This enhanced apparent processivity of PriA might play an important role in generating single-stranded DNA at stalled replication forks upon which to load DnaB. However, stimulation of PriA by PriB is not DNA structure-specific, demonstrating that targeting of stalled forks and recombination intermediates during replication restart likely resides with PriA alone.

Received for publication, August 3, 2005 , and in revised form, September 26, 2005.

^* This work was supported by the Medical Research Council and Biotechnology and Biological Sciences Research Council (to P. M.), National Institutes of Health Grant GM073495 (to M. L.), and a Shaw Scientist grant (to J. L. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Lister Institute-Jenner Research Fellow. To whom correspondence should be addressed: School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK. Tel.: 44-1224-555183; Fax: 44-1224-555844; E-mail: p.mcglynn{at}abdn.ac.uk.

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