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 language | English (US) |
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Pages (from-to) | 769-776 |
Number of pages | 8 |
Journal | EMBO Journal |
Volume | 11 |
Issue number | 2 |
State | Published - 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