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

Roxana E Georgescu, Isabel Kurth, Mike E O'Donnell

The Rockefeller University, Howard Hughes Medical Institute, New York, New York, USA.

Nature structural & molecular biology 2012 Jan

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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.

Citation

Roxana E Georgescu, Isabel Kurth, Mike E O'Donnell. Single-molecule studies reveal the function of a third polymerase in the replisome. Nature structural & molecular biology. 2012 Jan;19(1):113-6