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Nucleic Acids Res. 2006;34(15):4126-37. Epub 2006 Aug 25.

A dynamic model for replication protein A (RPA) function in DNA processing pathways.

Author information

1
Department of Biological Sciences, Vanderbilt University, VU Station B 351634, Nashville, TN 37235-1634, USA. ellen.fanning@vanderbilt.edu

Abstract

Processing of DNA in replication, repair and recombination pathways in cells of all organisms requires the participation of at least one major single-stranded DNA (ssDNA)-binding protein. This protein protects ssDNA from nucleolytic damage, prevents hairpin formation and blocks DNA reannealing until the processing pathway is successfully completed. Many ssDNA-binding proteins interact physically and functionally with a variety of other DNA processing proteins. These interactions are thought to temporally order and guide the parade of proteins that 'trade places' on the ssDNA, a model known as 'hand-off', as the processing pathway progresses. How this hand-off mechanism works remains poorly understood. Recent studies of the conserved eukaryotic ssDNA-binding protein replication protein A (RPA) suggest a novel mechanism by which proteins may trade places on ssDNA by binding to RPA and mediating conformation changes that alter the ssDNA-binding properties of RPA. This article reviews the structure and function of RPA, summarizes recent studies of RPA in DNA replication and other DNA processing pathways, and proposes a general model for the role of RPA in protein-mediated hand-off.

PMID:
16935876
PMCID:
PMC1616954
DOI:
10.1093/nar/gkl550
[Indexed for MEDLINE]
Free PMC Article

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