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. 1992 Feb;11(2):769-76.
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, I U Gilbert, D von Winkler, T J Kelly, E Fanning
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Interaction of DNA polymerase alpha-primase with cellular replication protein A and SV40 T antigen

I Dornreiter et al. EMBO J. 1992 Feb.

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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