4.8 Article

Single-molecule view of coordination in a multi-functional DNA polymerase

期刊

ELIFE
卷 10, 期 -, 页码 -

出版社

ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.62046

关键词

-

类别

资金

  1. National Institute of General Medical Sciences [RO1 GM044060, F32 GM115017]
  2. National Institute of Allergy and Infectious Diseases [T32 AI007354]

向作者/读者索取更多资源

The study using single-molecule FRET microscopy revealed that the 5' nuclease domain in DNA polymerase I (Pol I) from Escherichia coli adopts different positions within Pol I-DNA complexes depending on the nature of the DNA substrate, indicating the structural dynamics underlying functional coordination in Pol I.
Replication and repair of genomic DNA requires the actions of multiple enzymatic functions that must be coordinated in order to ensure efficient and accurate product formation. Here, we have used single-molecule FRET microscopy to investigate the physical basis of functional coordination in DNA polymerase I (Pol I) from Escherichia coli, a key enzyme involved in lagging-strand replication and base excision repair. Pol I contains active sites for template-directed DNA polymerization and 5' flap processing in separate domains. We show that a DNA substrate can spontaneously transfer between polymerase and 5' nuclease domains during a single encounter with Pol I. Additionally, we show that the flexibly tethered 5' nuclease domain adopts different positions within Pol I-DNA complexes, depending on the nature of the DNA substrate. Our results reveal the structural dynamics that underlie functional coordination in Pol I and are likely relevant to other multi-functional DNA polymerases.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据