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. 1992 Feb;11(2):769–776. doi: 10.1002/j.1460-2075.1992.tb05110.x

Interaction of DNA polymerase alpha-primase with cellular replication protein A and SV40 T antigen.

I Dornreiter 1, L F Erdile 1, I U Gilbert 1, D von Winkler 1, T J Kelly 1, E Fanning 1
PMCID: PMC556510  PMID: 1311258

Abstract

The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase alpha-primase, as shown by ELISA and a modified immunoblotting technique. RP-A associated efficiently with the isolated primase, as well as with intact polymerase alpha-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase alpha-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiating of SV40 DNA replication.

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Selected References

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