Structure of a DNA polymerase alpha-primase domain that docks on the SV40 helicase and activates the viral primosome.

ABSTRACT: DNA polymerase alpha-primase (pol-prim) plays a central role in DNA replication in higher eukaryotes, initiating synthesis on both leading and lagging strand single-stranded DNA templates. Pol-prim consists of a primase heterodimer that synthesizes RNA primers, a DNA polymerase that extends them, and a fourth subunit, p68 (also termed B-subunit), that is thought to regulate the complex. Although significant knowledge about single-subunit primases of prokaryotes has accumulated, the functions and regulation of pol-prim remain poorly understood. In the SV40 replication model, the p68 subunit is required for primosome activity and binds directly to the hexameric viral helicase T antigen, suggesting a functional link between T antigen-p68 interaction and primosome activity. To explore this lin

SUBMITTER: Huang H 

PROVIDER: S-EPMC2878050 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature