复制蛋白A最大亚基的不同活性在猴病毒40（SV40）DNA复制过程中协同发挥作用。
Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication.
作者信息
Taneja Poonam, Boche Irene, Hartmann Hella, Nasheuer Heinz-Peter, Grosse Frank, Fanning Ellen, Weisshart Klaus
机构信息
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA.
出版信息
FEBS Lett. 2007 Aug 21;581(21):3973-8. doi: 10.1016/j.febslet.2007.07.038. Epub 2007 Jul 25.
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.
复制蛋白A（RPA）是一种由p70、p32和p14亚基组成的稳定异源三聚体复合物。该蛋白在SV40微型染色体复制中起关键作用。代表较小两个亚基相互作用位点的p70肽、DNA以及病毒起始蛋白大T抗原（Tag）和细胞DNA聚合酶α-引发酶（Pol）均干扰了复制过程，表明不同的p70活性在此过程中的重要性。仅在引物合成前的起始前阶段观察到破坏蛋白质-蛋白质相互作用的肽的抑制作用，这表明在引物末端RPA、Tag和Pol之间形成了稳定的起始复合物。
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