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A Specific Docking Site for DNA Polymerase α-Primase on the SV40 Helicase Is Required for Viral Primosome Activity, but Helicase Activity Is Dispensable.

J Biol Chem.. 2010-10;  285(43):33475 - 33484
Hao Huang, Kun Zhao, Diana R. Arnett, and Ellen Fanning. Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235-1634, USA.
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Replication of simian virus 40 (SV40) DNA, a model for eukaryotic chromosomal replication, can be reconstituted in vitro using the viral helicase (large tumor antigen, or Tag) and purified human proteins. Tag interacts physically with two cellular proteins, replication protein A and DNA polymerase α-primase (pol-prim), constituting the viral primosome. Like the well characterized primosomes of phages T7 and T4, this trio of proteins coordinates parental DNA unwinding with primer synthesis to initiate the leading strand at the viral origin and each Okazaki fragment on the lagging strand template. We recently determined the structure of a previously unrecognized pol-prim domain (p68N) that docks on Tag, ide... More


DNA Helicase; DNA Polymerase; DNA Primase; DNA Replication; Protein-Protein Interactions; DNA Polymerase alpha-Primase; SV4 Replication; Helicase-Primase Coupling; Initiation; Modular Protein Interactions