Unknown

Dataset Information

0

Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication.


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 alpha-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.

SUBMITTER: Taneja P 

PROVIDER: S-EPMC2045582 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication.

Taneja Poonam P   Boche Irene I   Hartmann Hella H   Nasheuer Heinz-Peter HP   Grosse Frank F   Fanning Ellen E   Weisshart Klaus K  

FEBS letters 20070725 21


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 alpha-primase (Pol) all interfered with the replication process indicating the importance of the different p70 activities in this process. Inhibition by  ...[more]

Similar Datasets

| S-EPMC3617017 | biostudies-literature
| S-EPMC2049014 | biostudies-literature
| S-EPMC1345677 | biostudies-literature
| S-EPMC402079 | biostudies-other
| S-EPMC420356 | biostudies-literature
| S-EPMC2862297 | biostudies-literature
| S-EPMC7144908 | biostudies-literature
| S-EPMC3897190 | biostudies-literature
| S-EPMC4122284 | biostudies-literature
| S-EPMC1995709 | biostudies-literature