Structure and conformational change of a replication protein A heterotrimer bound to ssDNA Journal Article


Authors: Fan, J.; Pavletich, N. P.
Article Title: Structure and conformational change of a replication protein A heterotrimer bound to ssDNA
Abstract: Replication protein A (RPA) is the main eukaryotic ssDNA-binding protein with essential roles in DNA replication, recombination, and repair. RPA maintains the DNA as single-stranded and also interacts with other DNA-processing proteins, coordinating their assembly and disassembly on DNA. RPA binds to ssDNA in two conformational states with opposing affinities for DNA and proteins. The RPA-protein interactions are compatible with a low DNA affinity state that involves DNA-binding domain A (DBD-A) and DBD-B but not with the high DNA affinity state that additionally engages DBD-C and DBD-D. The structure of the high-affinity RPA-ssDNA complex reported here shows a compact quaternary structure held together by a four-way interface between DBD-B, DBD-C, the intervening linker (BC linker), and ssDNA. The BC linker binds into the DNAbinding groove of DBD-B, mimicking DNA. The associated conformational change and partial occlusion of the DBD-A-DBA-B protein-protein interaction site establish a mechanism for the allosteric coupling of RPA-DNA and RPA-protein interactions. © 2012 by Cold Spring Harbor Laboratory Press.
Keywords: controlled study; protein expression; nonhuman; binding affinity; dna replication; protein conformation; animal cell; dna recombination; dna repair; protein protein interaction; cell line; protein binding; models, molecular; protein structure, tertiary; replication factor a; single stranded dna; dna, single-stranded; nucleic acid conformation; protein structure; dna binding; replication protein a; protein dna interaction; allosterism; cross coupling reaction; fungal proteins; insect cell; ustilago; rpa; ssdna binding
Journal Title: Genes and Development
Volume: 26
Issue: 20
ISSN: 0890-9369
Publisher: Cold Spring Harbor Laboratory Press  
Date Published: 2012-10-15
Start Page: 2337
End Page: 2347
Language: English
DOI: 10.1101/gad.194787.112
PROVIDER: scopus
PMCID: PMC3475805
PUBMED: 23070815
DOI/URL:
Notes: --- - "Export Date: 2 November 2012" - "CODEN: GEDEE" - "Source: Scopus"
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  1. Jie Fan
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