Clamping Pol ε to the leading strand

IF 12.5 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Nature Structural & Molecular Biology Pub Date : 2024-10-22 DOI:10.1038/s41594-024-01416-1

Noopur Singh, Erik Johansson

引用次数: 0

Abstract

Two recent studies provide structural insights into how human DNA polymerase ε (Pol ε) interacts with PCNA to form a processive holoenzyme on the leading strand. A series of cryo-EM images offer structural information on the proofreading process, showing how DNA is transferred between the polymerase and exonuclease sites in human Pol ε.

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将 Pol ε 夹在前导链上

最近的两项研究从结构上揭示了人类DNA聚合酶ε（Pol ε）如何与PCNA相互作用，在前导链上形成一个过程性全酶。一系列低温电子显微镜图像提供了校对过程的结构信息，显示了人类 Pol ε 中 DNA 如何在聚合酶和外切酶位点之间转移。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Nature Structural & Molecular Biology BIOCHEMISTRY & MOLECULAR BIOLOGY-BIOPHYSICS

CiteScore

22.00

自引率

1.80%

发文量

160

审稿时长

3-8 weeks

期刊介绍： Nature Structural & Molecular Biology is a comprehensive platform that combines structural and molecular research. Our journal focuses on exploring the functional and mechanistic aspects of biological processes, emphasizing how molecular components collaborate to achieve a particular function. While structural data can shed light on these insights, our publication does not require them as a prerequisite.