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

I. Dornreiter, L. F. Erdile, L. U. Gilbert, D. Von Winkler, T. J. Kelly, E. Fanning

Research output: Contribution to journalArticlepeer-review

275 Scopus citations


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 α-primase, as shown by ELISA and a modified immunoblotting technique, RP-A associated efficiently with the isolated primase, as well as with intact polymerase α-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase α-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 initiation of SV40 DNA replication.

Original languageEnglish (US)
Pages (from-to)769-776
Number of pages8
JournalEMBO Journal
Issue number2
StatePublished - 1992
Externally publishedYes


  • DNA polymerase α
  • Initiation of DNA replication
  • Protein-protein interactions
  • SV40 T antigen
  • Single-strand DNA binding protein

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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