RNAP II CTD Phosphorylated on Threonine-4 Is Required for Histone mRNA 3′ End Processing

被引：117
作者：
Hsin, Jing-Ping [1 ]
Sheth, Amit [1 ]
Manley, James L. [1 ]
机构：
[1] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA
来源：
SCIENCE | 2011年 / 334卷 / 6056期
关键词：
CARBOXYL-TERMINAL DOMAIN; POLYMERASE-II; GENE-EXPRESSION; P-TEFB; TRANSCRIPTION; SERINE-7; ASF/SF2; EVENTS;
D O I：
10.1126/science.1206034
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The RNA polymerase II (RNAP II) largest subunit contains a C-terminal domain (CTD) with up to 52 Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7) consensus repeats. Serines 2, 5, and 7 are known to be phosphorylated, and these modifications help to orchestrate the interplay between transcription and processing of messenger RNA (mRNA) precursors. Here, we provide evidence that phosphorylation of CTD Thr(4) residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes. Like Ser(2), Thr(4) phosphorylation requires the CTD kinase CDK9 and is evolutionarily conserved from yeast to human. Our data thus illustrate how a CTD modification can play a highly specific role in facilitating efficient gene expression.
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收藏
页码：683 / 686
页数：4
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