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

Irene Dornreiter, Lome F. Erdile, Ilka U. Gilbert, Dorothea Von Winkler, Thomas J. Kelly, Ellen Fanning

Research output: Contribution to journalArticlepeer-review

275 Scopus citations

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 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 a-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
Volume11
Issue number2
StatePublished - 1992

Keywords

  • DNA polymerase α
  • Initiation of DNA replication
  • Protein-protein interactions
  • Single-strand DNA binding proteinSV40 T antigen

ASJC Scopus subject areas

  • General Immunology and Microbiology
  • General Biochemistry, Genetics and Molecular Biology
  • Molecular Biology
  • General Neuroscience

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