Structural basis for the recognition of the S2, S5-phosphorylated RNA polymerase II CTD by the mRNA anti-terminator protein hSCAF4

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成果类型：

期刊论文

作者：

Zhou, Mengqi;Ehsan, Fahad;Gan, Linyao;Dong, Aiping;Li, Yanjun;...

通讯作者：

Liu, Ke;Min, Jinrong

作者机构：

[Liu, Ke; Min, Jinrong; Gan, Linyao; Zhou, Mengqi] Cent China Normal Univ, Sch Life Sci, Hubei Key Lab Genet Regulat & Integrat Biol, Wuhan 430079, Hubei, Peoples R China.

[Dong, Aiping; Ehsan, Fahad; Li, Yanjun; Zhou, Mengqi; Min, Jinrong] Univ Toronto, Struct Genom Consortium, Toronto, ON, Canada.

[Ehsan, Fahad; Min, Jinrong] Univ Toronto, Dept Physiol, Toronto, ON, Canada.

通讯机构：

[Liu, K; Min, JR] C

Cent China Normal Univ, Sch Life Sci, Hubei Key Lab Genet Regulat & Integrat Biol, Wuhan 430079, Hubei, Peoples R China.

语种：

英文

关键词：

CTD interaction domain;hSCAF4;isothermal titration calorimetry;phosphorylated CTD;X-ray crystallography

期刊：

FEBS Letters

ISSN：

0014-5793

年：

2022

卷：

596

期：

页码：

249-259

DOI：

10.1002/1873-3468.14256

基金类别：

Natural Sciences and Engineering Research CouncilNatural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2016-06300]; Structural Genomics ConsortiumUniversity of Toronto; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31770834]; Central China Normal University (CCNU) from the college's basic research and operation of Ministry of Education (MOE) [KJ02072019-0346]; Boehringer IngelheimBoehringer Ingelheim [1097737]; AbbVieAbbVie [1097737]; Canadian Institutes of Health Research (CIHR)Canadian Institutes of Health Research (CIHR) [1097737]; Genome CanadaGenome Canada [1097737]; Ontario Genomics Institute [1097737, OGI-055]

机构署名：

本校为第一且通讯机构

院系归属：

生命科学学院

摘要：

The C-terminal domain (CTD) of RNA polymerase II serves as a binding platform for numerous enzymes and transcription factors involved in nascent RNA processing and the transcription cycle. The S2, S5-phosphorylated CTD is recognized by the transcription factor SCAF4, which functions as a transcription anti-terminator by preventing early mRNA transcript cleavage and polyadenylation. Here, we measured the binding affinities of differently modified CTD peptides by hSCAF4 and solved the complex structure of the hSCAF4-CTD-interaction domain (CID) b...

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Structural basis for the recognition of the S2, S5-phosphorylated RNA polymerase II CTD by the mRNA anti-terminator protein hSCAF4

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