Single-molecule studies reveal the function of a third polymerase in the replisome.

ABSTRACT: The Escherichia coli replisome contains three polymerases, one more than necessary to duplicate the two parental strands. Using single-molecule studies, we reveal two advantages conferred by the third polymerase. First, dipolymerase replisomes are inefficient at synthesizing lagging strands, leaving single-strand gaps, whereas tripolymerase replisomes fill strands almost to completion. Second, tripolymerase replisomes are much more processive than dipolymerase replisomes. These features account for the unexpected three-polymerase-structure of bacterial replisomes.

SUBMITTER: Georgescu RE 

PROVIDER: S-EPMC3721970 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature