Literature DB >> 1311258

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

I Dornreiter1, L F Erdile, I U Gilbert, D von Winkler, T J Kelly, E Fanning.   

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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Year:  1992        PMID： 1311258      PMCID： PMC556510          DOI： 10.1002/j.1460-2075.1992.tb05110.x

Source DB:  PubMed          Journal:  EMBO J        ISSN： 0261-4189            Impact factor:   11.598


  54 in total

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