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
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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。
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来源期刊
Nature Structural & Molecular Biology
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.
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