| Literature DB >> 22918591 |
Lynne M Dieckman1, Bret D Freudenthal, M Todd Washington.
Abstract
Proliferating cell nuclear antigen (PCNA), the eukaryotic DNA sliding clamp, forms a ring-shaped homo-trimer that encircles double-stranded DNA. This protein is best known for its ability to confer high processivity to replicative DNA polymerases. However, it does far more than this, because it forms a mobile platform on the DNA that recruits many of the proteins involved in DNA replication, repair, and recombination to replication forks. X-ray crystal structures of PCNA bound to PCNA-binding proteins have provided insights into how PCNA recognizes its binding partners and recruits them to replication forks. More recently, X-ray crystal structures of ubiquitin-modified and SUMO-modified PCNA have provided insights into how these post-translational modifications alter the specificity of PCNA for some of its binding partners. This article focuses on the insights gained from structural studies of PCNA complexes and post-translationally modified PCNA.Entities:
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Year: 2012 PMID: 22918591 PMCID: PMC4429884 DOI: 10.1007/978-94-007-4572-8_15
Source DB: PubMed Journal: Subcell Biochem ISSN: 0306-0225