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Taneja, P,Boche, I,Hartmann, H,Nasheuer, HP,Grosse, F,Fanning, E,Weisshart, K
2007
August
Febs Letters
Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication
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SV40 DNA replication replication protein a protein-protein interaction SINGLE-STRANDED-DNA LARGE T-ANTIGEN BINDING DOMAIN POLYMERASE-ALPHA MULTIPLE STAGES INITIATION MECHANISM INVITRO RPA IDENTIFICATION
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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 a-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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
DOI 10.1016/j.febslet.2007.07.038
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