Rep Provides a Second Motor at the Replisome to Promote Duplication of Protein-bound DNA

Overview

Journal Mol Cell

Publisher Cell Press

Specialty Cell Biology

Date 2009 Nov 28

PMID 19941825

Citations 105

Authors

Colin P Guy

John Atkinson

Milind K Gupta

Akeel A Mahdi

Emma J Gwynn

Christian J Rudolph

Peter B Moon

Ingeborg C van Knippenberg

Chris J Cadman

Mark S Dillingham

Robert G Lloyd

Peter McGlynn

Affiliations

Soon will be listed here.

Abstract

Nucleoprotein complexes present challenges to genome stability by acting as potent blocks to replication. One attractive model of how such conflicts are resolved is direct targeting of blocked forks by helicases with the ability to displace the blocking protein-DNA complex. We show that Rep and UvrD each promote movement of E. coli replisomes blocked by nucleoprotein complexes in vitro, that such an activity is required to clear protein blocks (primarily transcription complexes) in vivo, and that a polarity of translocation opposite that of the replicative helicase is critical for this activity. However, these two helicases are not equivalent. Rep but not UvrD interacts physically and functionally with the replicative helicase. In contrast, UvrD likely provides a general means of protein-DNA complex turnover during replication, repair, and recombination. Rep and UvrD therefore provide two contrasting solutions as to how organisms may promote replication of protein-bound DNA.

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