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Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication
Author(s) -
Taneja Poonam,
Boche Irene,
Hartmann Hella,
Nasheuer Heinz-Peter,
Grosse Frank,
Fanning Ellen,
Weisshart Klaus
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.038
Subject(s) - minichromosome maintenance , replication factor c , origin recognition complex , replication protein a , dna replication , pre replication complex , eukaryotic dna replication , dna replication factor cdt1 , heterotrimeric g protein , primer (cosmetics) , microbiology and biotechnology , biology , seqa protein domain , processivity , protein subunit , control of chromosome duplication , chemistry , dna , genetics , dna binding protein , gene , g protein , signal transduction , organic chemistry , transcription factor
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.