TY - JOUR
T1 - PCNA structure and function
T2 - Insights from structures of PCNA complexes and post-translationally modi fied PCNA
AU - Dieckman, Lynne M.
AU - Freudenthal, Bret D.
AU - Washington, M. Todd
N1 - Funding Information:
This article was supported by Award Number GM081433 from the National Institute of General Medical Sciences to M.T.W. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of General Medical sciences or the National Institutes of Health. We thank Christine Kondratick, John Pryor and Marc Wold for valuable discussions.
Publisher Copyright:
© Springer Science+Business Media Dordrecht 2012.
PY - 2012/5/29
Y1 - 2012/5/29
N2 - 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.
AB - 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.
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U2 - 10.1007/978-94-007-4572-8_15
DO - 10.1007/978-94-007-4572-8_15
M3 - Article
C2 - 22918591
AN - SCOPUS:84875398809
VL - 62
SP - 281
EP - 299
JO - Sub-Cellular Biochemistry
JF - Sub-Cellular Biochemistry
SN - 0306-0225
ER -