Functional identity of proliferating cell nuclear antigen and a DNA polymerase-δ auxiliary protein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-04

AUTHORS

Gregory Prelich, Cheng-Keat Tan, Matthew Kostura, Michael B. Mathews, Antero G. So, Kathleen M. Downey, Bruce Stillman

ABSTRACT

The mechanism of replication of the simian virus 40 (SV40) genome closely resembles that of cellular chromosomes, thereby providing an excellent model system for examining the enzymatic requirements for DNA replication. Only one viral gene product, the large tumour antigen (large-T antigen), is required for viral replication, so the majority of replication enzymes must be cellular. Indeed, a number of enzymatic activities associated with replication and the S phase of the cell cycle are induced upon SV40 infection. Cell-free extracts derived from human cells, when supplemented with immunopurified SV40 large-T antigen support efficient replication of plasmids that contain the SV40 origin of DNA replication. Using this system, a cellular protein of relative molecular mass 36,000 (Mr = 36K) that is required for the elongation stage of SV40 DNA replication in vitro has been purified and identified as a known cell-cycle regulated protein, alternatively called the proliferating cell nuclear antigen (PCNA) or cyclin. It was noticed that, in its physical characteristics, PCNA closely resembles a protein that regulates the activity of calf thymus DNA polymerase-delta. Here we show that PCNA and the polymerase-delta auxiliary protein have similar electrophoretic behaviour and are both recognized by anti-PCNA human autoantibodies. More importantly, both proteins are functionally equivalent; they stimulate SV40 DNA replication in vitro and increase the processivity of calf thymus DNA polymerase-delta. These results implicate a novel animal cell DNA polymerase, DNA polymerase-delta, in the elongation stage of replicative DNA synthesis in vitro. More... »

PAGES

517-520

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/326517a0

DOI

http://dx.doi.org/10.1038/326517a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025445753

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2882424


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