The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart Journal Article


Authors: Heller, R. C.; Marians, K. J.
Article Title: The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart
Abstract: Rescue of arrested and collapsed replication forks is essential for maintenance of genomic integrity. One system for origin of replication- independent loading of the DnaB replicative helicase and subsequent replisome reassembly requires the structure-specific recognition factor PriA and the assembly factors PriB and DnaT. Here, we provide biochemical evidence for an alternate system for DnaB loading that requires only PriC. Furthermore, the choice of which system is utilized during restart is dictated by the nature of the structure of the stalled replication fork. PriA-dependent reactions are most robust on fork structures with no gaps in the leading strand, such as is found at the junction of a D loop, while the PriC-dependent system preferentially utilizes fork structures with large gaps in the leading strand. These observations suggest that the type of initial damage on the DNA template and how the inactivated fork is processed ultimately influence the choice of enzymatic restart pathway. Copyright © 2005 by Elsevier Inc.
Keywords: protein expression; dna-binding proteins; nonhuman; chemical analysis; dna replication; dna damage; dose-response relationship, drug; bacterial proteins; dna; escherichia coli; genome; helicase; protein structure; adenosine triphosphatases; dna helicases; escherichia coli proteins; dna template; replisome; disposable equipment; deoxyribonucleoprotein; dnab helicases
Journal Title: Molecular Cell
Volume: 17
Issue: 5
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2005-03-04
Start Page: 733
End Page: 743
Language: English
DOI: 10.1016/j.molcel.2005.01.019
PUBMED: 15749022
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 61" - "Export Date: 24 October 2012" - "CODEN: MOCEF" - "Source: Scopus"
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  1. Kenneth Marians
    129 Marians