Identification of regions within the four small subunits of human replication factor C required for complex formation and DNA replication Journal Article


Authors: Uhlmann, F.; Gibbs, E.; Cai, J.; O'Donnell, M.; Hurwitz, J.
Article Title: Identification of regions within the four small subunits of human replication factor C required for complex formation and DNA replication
Abstract: Replication factor C (RFC) and proliferating cell nuclear antigen (PCNA) are processivity factors for eukoryotic DNA polymerases δ and ε. RFC binds to a DNA primer end and loads PCNA onto DNA in an ATP-dependent reaction. The five RFC subunits p140, p40, p38, p37, and p36, all of which are required to form the active RFC complex, share regions of high homology including the defined RFC boxes II-VIII. RFC boxes III and V constitute a putative ATP binding site, whereas the function of the other conserved boxes is unknown. To study the individual subunits in the RFC complex and the role of the RFC boxes, deletion mutations were created in all subunits. Sequences close to the C terminus of each of the small subunits are required for formation of the five subunit complex. A N-terminal region of the small subunits, containing the RFC homology box II, plays a critical role in the function of these subunits, deletion of which reduces but does not abolish RFC activity in loading PCNA onto DNA and in supporting an RFC-dependent replication reaction. The N termini of p37 and p40, although highly homologous, are not interchangeable, suggesting unique functions for the individual subunits.
Keywords: controlled study; human cell; dna-binding proteins; sequence deletion; dna polymerase; dna replication; protein conformation; complex formation; dna repair; genetic transcription; homeodomain proteins; hela cell; structure-activity relationship; recombinant fusion proteins; saccharomyces cerevisiae proteins; adenosine triphosphate; cycline; replication protein c; dna binding; repressor proteins; proto-oncogene proteins c-bcl-2; deletion mutant; proliferating cell nuclear antigen; dna, circular; humans; human; priority journal; article
Journal Title: Journal of Biological Chemistry
Volume: 272
Issue: 15
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1997-04-11
Start Page: 10065
End Page: 10071
Language: English
DOI: 10.1074/jbc.272.15.10065
PUBMED: 9092550
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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  1. Jerard Hurwitz
    206 Hurwitz
  2. Emma Gibbs
    14 Gibbs
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