Dynamic DNA helicase-DNA polymerase interactions assure processive replication fork movement

被引：88

作者：

Hamdan, Samir M. ^{[1
]}

Johnson, Donald E. ^{[1
]}

Tanner, Nathan A. ^{[1
]}

Lee, Jong-Bong ^{[1
]}

Qimron, Udi ^{[1
]}

Tabor, Stanley ^{[1
]}

van Oijen, Antoine M. ^{[1
]}

Richardson, Charles C. ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

MOLECULAR CELL | 2007年 / 27卷 / 04期

关键词：

D O I：

10.1016/j.molcel.2007.06.020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A single copy of bacteriophage T7 DNA polymerase and DNA helicase advance the replication fork with a processivity greater than 17,000 nucleoticles. Nonetheless, the polymerase transiently dissociates from the DNA without leaving the replisome. Ensemble and single-molecule techniques demonstrate that this dynamic processivity is made possible by two modes of DNA polymerase-helicase interaction. During DNA synthesis the polymerase and the helicase interact at a high-affinity site. In this polymerizing mode, the polymerase dissociates from the DNA approximately every 5000 bases. The polymerase, however, remains bound to the helicase via an electrostatic binding mode that involves the acidic C-terminal tail of the helicase and a basic region in the polymerase to which the processivity factor also binds. The polymerase transfers via the electrostatic interaction around the hexameric helicase in search of the primer-template.

引用

页码：539 / 549

页数：11

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