Unwinding of the nascent lagging strand by Rep and PriA enables the direct restart of stalled replication forks Journal Article


Authors: Heller, R. C.; Marians, K. J.
Article Title: Unwinding of the nascent lagging strand by Rep and PriA enables the direct restart of stalled replication forks
Abstract: During origin-independent replisome assembly, the replication restart protein PriC prefers to load the replication fork helicase, DnaB, to stalled replication forks where there is a gap in the nascent leading strand. However, this activity can be obstructed if the 5′-end of the nascent lagging strand is near the template branch point. Here we provide biochemical evidence that the helicase activities of Rep and PriA function to unwind the nascent lagging strand DNA at such stalled replication forks. PriC then loads the replicative helicase, DnaB, onto the newly generated, single-stranded template for the purposes of replisome assembly and duplex unwinding ahead of the replication fork. Direct rescue of replication forks by the Rep-PriC and PriA-PriC pathways in this manner may contribute to genomic stability by avoiding the potential dangers of fork breakage inherent to recombination- dependent restart pathways. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Keywords: unclassified drug; dna-binding proteins; nonhuman; dna replication; protein function; dna recombination; genes; protein assembly; enzyme activity; dna strand breakage; dna; 5' untranslated region; recombination, genetic; trans-activators; helicase; dna replication origin; molecular biology; biochemistry; adenosine triphosphatases; enzymes; dna helicases; dna denaturation; dna template; self assembly; replisome; templates, genetic; protein pria; lagging strand; protein dnab; replisome assembly; stalled replication; protein pric
Journal Title: Journal of Biological Chemistry
Volume: 280
Issue: 40
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2005-10-07
Start Page: 34143
End Page: 34151
Language: English
DOI: 10.1074/jbc.M507224200
PUBMED: 16079128
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 41" - "Export Date: 24 October 2012" - "CODEN: JBCHA" - "Source: Scopus"
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  1. Kenneth Marians
    127 Marians