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.
| Original language | English |
|---|---|
| Pages (from-to) | 281-299 |
| Number of pages | 19 |
| Journal | Sub-Cellular Biochemistry |
| Volume | 62 |
| State | Published - 2012 |
| Externally published | Yes |
Fingerprint
All Science Journal Classification (ASJC) codes
- Medicine(all)
Cite this
PCNA structure and function : insights from structures of PCNA complexes and post-translationally modified PCNA. / Dieckman, Lynne; Freudenthal, Bret D.; Washington, M. Todd.
In: Sub-Cellular Biochemistry, Vol. 62, 2012, p. 281-299.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - PCNA structure and function
T2 - insights from structures of PCNA complexes and post-translationally modified PCNA.
AU - Dieckman, Lynne
AU - Freudenthal, Bret D.
AU - Washington, M. Todd
PY - 2012
Y1 - 2012
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
M3 - Review article
VL - 62
SP - 281
EP - 299
JO - Sub-Cellular Biochemistry
JF - Sub-Cellular Biochemistry
SN - 0306-0225
ER -