Multiple competition reactions for RPA order the assembly of the DNA polymerase δ holoenzyme Journal Article

   


Authors: Yuzhakov, A.; Kelman, Z.; Hurwitz, J.; O'Donnell, M.
Article Title: Multiple competition reactions for RPA order the assembly of the DNA polymerase δ holoenzyme
Abstract: Processive extension of DNA in eukaryotes requires three factors to coordinate their actions. First, DNA polymerase α-primase synthesizes the primed site. Then replication factor C loads a proliferating cell nuclear antigen (PCNA) clamp onto the primer. Following this, DNA polymerase δ assembles with PCNA for processive extension. This report shows that these proteins each bind the primed site tightly and trade places in a highly coordinated fashion such that the primer terminus is never left free of protein. Replication protein A (RPA), the single-stranded DNA-binding protein, forms a common touchpoint for each of these proteins and they compete with one another for it. Thus these protein exchanges are driven by competition-based protein switches in which two proteins vie for contact with RPA.
Keywords: dna binding protein; dna-binding proteins; dna replication; protein assembly; protein protein interaction; protein binding; homeodomain proteins; dna; kinetics; eukaryota; escherichia coli; saccharomyces cerevisiae proteins; replication factor c; cycline; dna, single-stranded; replication protein c; repressor proteins; proto-oncogene proteins c-bcl-2; replication protein a; protein dna interaction; proliferating cell nuclear antigen; dna directed dna polymerase delta; binding, competitive; dna primase; dna polymerase iii; humans; priority journal; article; dna polymerase δ
Journal Title: EMBO Journal
Volume: 18
Issue: 21
ISSN: 0261-4189
Publisher: Wiley Blackwell  
Date Published: 1999-11-01
Start Page: 6189
End Page: 6199
Language: English
DOI: 10.1093/emboj/18.21.6189
PUBMED: 10545128
PROVIDER: scopus
PMCID: PMC1171682
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033230401&partnerID=40&md5=a4b2a103838baf360baf2936aec4bcbe
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
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MSK Authors
  1. Jerard Hurwitz
    206 Hurwitz
  2. Zvi Kelman
    17 Kelman
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