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 - 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.
UR - http://www.scopus.com/inward/record.url?scp=84875398809&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84875398809&partnerID=8YFLogxK
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 -