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

Single-molecule studies reveal the function of a third polymerase in the replisome.
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DOI:
10.1038/nsmb.2179
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发表时间:
2011-12-11
影响因子:
16.8
通讯作者:
O'Donnell, Mike E.
O'Donnell, Mike E.
中科院分区:
生物学1区
文献类型:
--
作者:
Georgescu, Roxana E.;Kurth, Isabel;O'Donnell, Mike E.

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大肠杆菌复制体含有三种聚合酶,比复制两条亲本链所需的多一种。利用单分子研究,我们揭示了第三聚合酶的两个优势。首先,二聚合酶复制体在合成滞后链时效率低下,留下单链间隙,而三聚合酶复制体几乎完全填充链。其次,三聚合酶复制体比二聚合酶复制体更具进行性。这些特征解释了细菌复制体意想不到的三聚合酶结构。
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.
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