RNA聚合酶C末端结构域的结构和相分离Ⅱ。

IF 2.9 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Biological Chemistry Pub Date : 2023-06-20 Print Date: 2023-07-26 DOI:10.1515/hsz-2023-0136
Irina P Lushpinskaia, David Flores-Solis, Markus Zweckstetter
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引用次数: 0

摘要

RPB1是RNA聚合酶II(Pol II)的最大亚基,其C末端结构域(CTD)中的重复七肽在调节基于Pol II的转录中起着关键作用。通过冷冻电镜确定的起始前复合物中CTD的结构和关键转录组分的新相分离性质的最新发现为转录过程中Pol II的时空分布提供了扩展的机制解释。目前的实验证据进一步表明,CTD的局部结构和一系列多价相互作用之间存在着微妙的平衡,这些相互作用驱动Pol II的相分离,从而形成其转录活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structure and phase separation of the C-terminal domain of RNA polymerase II.

The repetitive heptads in the C-terminal domain (CTD) of RPB1, the largest subunit of RNA Polymerase II (Pol II), play a critical role in the regulation of Pol II-based transcription. Recent findings on the structure of the CTD in the pre-initiation complex determined by cryo-EM and the novel phase separation properties of key transcription components offers an expanded mechanistic interpretation of the spatiotemporal distribution of Pol II during transcription. Current experimental evidence further suggests an exquisite balance between CTD's local structure and an array of multivalent interactions that drive phase separation of Pol II and thus shape its transcriptional activity.

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来源期刊
Biological Chemistry
Biological Chemistry 生物-生化与分子生物学
CiteScore
7.20
自引率
0.00%
发文量
63
审稿时长
4-8 weeks
期刊介绍: Biological Chemistry keeps you up-to-date with all new developments in the molecular life sciences. In addition to original research reports, authoritative reviews written by leading researchers in the field keep you informed about the latest advances in the molecular life sciences. Rapid, yet rigorous reviewing ensures fast access to recent research results of exceptional significance in the biological sciences. Papers are published in a "Just Accepted" format within approx.72 hours of acceptance.
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