Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell. Naryzhny, S., Zhao, H., & Lee, H. Journal of Biological Chemistry, 280(14):13888-13894, 2005. cited By 42![Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 1 download The diverse function of proliferating cell nuclear antigen (PCNA) may be regulated by interactions with different protein partners. Interestingly, the binding sites for all known PCNA-associating proteins are on the outer surface or the C termini ("front") sides of the PCNA trimer. Using cell extracts and purified human PCNA protein, we show here that two PCNA homotrimers form a back-to-back doublet. Mutation analysis suggests that the Arg-5 and Lys-110 residues on the PCNA back side are the contact points of the two homotrimers in the doublet. Furthermore, short synthetic peptides encompassing either Arg-5 or Lys-110 inhibit double trimer formation. We also found that a PCNA double trimer, but not a homotrimer alone, can simultaneously accommodate chromatin assembly factor-1 and polymerase δ. Together, our data supports a model that chromatin remodeling by chromatin assembly factor-1 (and, possibly, many other cellular activities) are tightly coupled with DNA replication (and repair) through a PCNA double trimer complex. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
@ARTICLE{Naryzhny200513888,
author={Naryzhny, S.N. and Zhao, H. and Lee, H.},
title={Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell},
journal={Journal of Biological Chemistry},
year={2005},
volume={280},
number={14},
pages={13888-13894},
doi={10.1074/jbc.M500304200},
note={cited By 42},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-17144365007&doi=10.1074%2fjbc.M500304200&partnerID=40&md5=971337febe9ffc34c27ef1171f8bc74a},
affiliation={Department of Research, NE Ontario Regional Cancer Centre, Sudbury, Ont. P3E 5J1, Canada; Dept. of Research, NE Ontario Regional Cancer Centre, 41 Ramsey Lake Rd., Sudbury, Ont. P3E 5J1, Canada},
abstract={The diverse function of proliferating cell nuclear antigen (PCNA) may be regulated by interactions with different protein partners. Interestingly, the binding sites for all known PCNA-associating proteins are on the outer surface or the C termini ("front") sides of the PCNA trimer. Using cell extracts and purified human PCNA protein, we show here that two PCNA homotrimers form a back-to-back doublet. Mutation analysis suggests that the Arg-5 and Lys-110 residues on the PCNA back side are the contact points of the two homotrimers in the doublet. Furthermore, short synthetic peptides encompassing either Arg-5 or Lys-110 inhibit double trimer formation. We also found that a PCNA double trimer, but not a homotrimer alone, can simultaneously accommodate chromatin assembly factor-1 and polymerase δ. Together, our data supports a model that chromatin remodeling by chromatin assembly factor-1 (and, possibly, many other cellular activities) are tightly coupled with DNA replication (and repair) through a PCNA double trimer complex. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.},
correspondence_address1={Lee, H.; Dept. of Research, NE Ontario Regional Cancer Centre, 41 Ramsey Lake Rd., Sudbury, Ont. P3E 5J1, Canada; email: hlee@hrsrh.on.ca},
issn={00219258},
coden={JBCHA},
pubmed_id={15805117},
language={English},
abbrev_source_title={J. Biol. Chem.},
document_type={Article},
source={Scopus},
}
Downloads: 1
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