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The Human Homologue of Fission Yeast cdc27, p66, Is a Component of Active Human DNA Polymerase δ,1.
- Source :
- Journal of Biochemistry; 2001, Vol. 129 Issue 5, p699-708, 10p
- Publication Year :
- 2001
-
Abstract
- An essential eukaryotic DNA polymerase, DNA polymerase δ(pol δ), synthesizes DNA processively in the presence of proliferating cell nuclear antigen (PCNA). Recently, a 66 kDa polypeptide (p66) that displays significant homology within its PCNA binding domain to that of fission yeast cdc27 was identified as a component of mouse and calf thy-mus pol δ. Our studies show that p66 interacts tightly with other subunits of pol δ during size fractionation of human cell extracts, and co-immunoprecipitates with these sub-units along with PCNA-dependent polymerase activity. Active human pol δ could be reconstituted by co-expressing pl25, p50, and p66 recombinant baculoviruses, but not by co-expressing pl25 and p50 alone. Interaction studies demonstrated that p66 tabilizes the association between pl25 and p50. Pull-down assays with PCNA-linked beads demonstrated that p66 increases the overall affinity of pol 8 for PCNA. These results indicate that p66 is a functionally important subunit of human pol 8 that stabilizes the pol 8 complex and increases the affinity of pol δ for PCNA. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0021924X
- Volume :
- 129
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 80086541
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a002909