The puzzle of PCNA's many partners
- PMID: 11056476
- DOI: 10.1002/1521-1878(200011)22:11<997::AID-BIES6>3.0.CO;2-#
The puzzle of PCNA's many partners
Abstract
The identification of proteins that interact with proliferating cell nuclear antigen (PCNA) has recently been a rapidly expanding field of discovery. PCNA is involved in many aspects of DNA replication and processing, forming a sliding platform that can mediate the interaction of proteins with DNA. It is striking that many proteins bind to PCNA through a small region containing a conserved motif; these include proteins involved in cell cycle regulation as well as those involved in DNA processing. Sequential and regulated binding of motif-containing proteins to PCNA may contribute to the ordering of events during DNA replication and repair. Results from bacteriophages and archaea show that the structural basis for the interaction of this motif with PCNA is extremely ancient. The analysis of how such functional motifs have been recruited to proteins in present day organisms helps us to understand how these complex systems arose from ancestral organisms.
Similar articles
-
Proliferating cell nuclear antigen (PCNA): a dancer with many partners.J Cell Sci. 2003 Aug 1;116(Pt 15):3051-60. doi: 10.1242/jcs.00653. J Cell Sci. 2003. PMID: 12829735 Review.
-
Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair.Oncogene. 1997 May 15;14(19):2313-21. doi: 10.1038/sj.onc.1201072. Oncogene. 1997. PMID: 9178907
-
Proliferating cell nuclear antigen (PCNA): ringmaster of the genome.Int J Radiat Biol. 2001 Oct;77(10):1007-21. doi: 10.1080/09553000110069335. Int J Radiat Biol. 2001. PMID: 11682006 Review.
-
Two cell-cycle regulated SET-domain proteins interact with proliferating cell nuclear antigen (PCNA) in Arabidopsis.Plant J. 2006 Aug;47(3):395-407. doi: 10.1111/j.1365-313X.2006.02799.x. Epub 2006 Jun 12. Plant J. 2006. PMID: 16771839
-
Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex.Nat Genet. 2000 Nov;26(3):375-8. doi: 10.1038/81708. Nat Genet. 2000. PMID: 11062484
Cited by
-
Unraveling molecular effects of ADAR1 overexpression in HEK293T cells by label-free quantitative proteomics.Cell Cycle. 2016 Jun 17;15(12):1591-601. doi: 10.1080/15384101.2016.1176657. Epub 2016 Apr 22. Cell Cycle. 2016. PMID: 27104882 Free PMC article.
-
A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11627-32. doi: 10.1073/pnas.191384398. Proc Natl Acad Sci U S A. 2001. PMID: 11573000 Free PMC article.
-
Characterization of dRFX2, a novel RFX family protein in Drosophila.Nucleic Acids Res. 2004 Oct 19;32(18):5636-48. doi: 10.1093/nar/gkh895. Print 2004. Nucleic Acids Res. 2004. PMID: 15494451 Free PMC article.
-
An in vivo analysis of the localisation and interactions of human p66 DNA polymerase delta subunit.BMC Mol Biol. 2005 Jul 6;6:17. doi: 10.1186/1471-2199-6-17. BMC Mol Biol. 2005. PMID: 16000169 Free PMC article.
-
Structural and biochemical studies of human proliferating cell nuclear antigen complexes provide a rationale for cyclin association and inhibitor design.Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1871-6. doi: 10.1073/pnas.0406540102. Epub 2005 Jan 28. Proc Natl Acad Sci U S A. 2005. PMID: 15681588 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous