Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872567 | FEBS Letters | 2007 | 6 Pages |
Abstract
Replication protein A (RPA) is a stable heterotrimeric complex consisting of p70, p32 and p14 subunits. The protein plays a crucial role in SV40 minichromosome replication. Peptides of p70 representing interaction sites for the smaller two subunits, DNA as well as the viral initiator protein large T-antigen (Tag) and the cellular DNA polymerase α-primase (Pol) all interfered with the replication process indicating the importance of the different p70 activities in this process. Inhibition by the peptide disrupting protein-protein interactions was observed only during the pre-initiation stage prior to primer synthesis, suggesting the formation of a stable initiation complex between RPA, Tag and Pol at the primer end.
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Authors
Poonam Taneja, Irene Boche, Hella Hartmann, Heinz-Peter Nasheuer, Frank Grosse, Ellen Fanning, Klaus Weisshart,