Making 3′ ends meet

IF 10.1 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Nature Structural & Molecular Biology Pub Date : 2025-05-22 DOI:10.1038/s41594-025-01578-6

Sylvie Doublié

引用次数: 0

Abstract

Two papers offer a first glimpse at complexes of the helicase-like domain of DNA polymerase θ (Polθ-HD) bound to DNA. Together, they provide structural insights into how the dimeric form of Polθ-HD grabs and aligns single-stranded DNA tails near the 3′ termini, a process that is accompanied by large conformational changes within Polθ-HD.

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两篇论文提供了DNA聚合酶θ (Polθ-HD)的解旋酶样结构域与DNA结合的复合体的第一眼。他们共同提供了关于Polθ-HD二聚体形式如何在3 '末端附近捕获和排列单链DNA尾巴的结构见解，这一过程伴随着Polθ-HD内部的大构象变化。

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.