Rtr1 Is a CTD Phosphatase that Regulates RNA Polymerase II during the Transition from Serine 5 to Serine 2 Phosphorylation

被引：117

作者：

Mosley, Amber L. ^{[1
]}

Pattenden, Samantha G. ^{[1
]}

Carey, Michael ^{[1
,2
]}

Venkatesh, Swaminathan ^{[1
]}

Gilmore, Joshua M. ^{[1
]}

Florens, Laurence ^{[1
]}

Workman, Jerry L. ^{[1
]}

Washburn, Michael P. ^{[1
]}

机构：

[1] Stowers Inst Med Res, Kansas City, MO 64110 USA

[2] Univ Calif Los Angeles, David Geffen Sch Med, Dept Biol Chem, Los Angeles, CA 90095 USA

来源：

MOLECULAR CELL | 2009年 / 34卷 / 02期

关键词：

C-TERMINAL DOMAIN; MESSENGER-RNA; TRANSCRIPTION TERMINATION; SYSTEMATIC ANALYSIS; PROCESSING FACTORS; FCP1; PHOSPHATASE; CAPPING ENZYME; KINASE-I; PROTEIN; SSU72;

D O I：

10.1016/j.molcel.2009.02.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Messenger RNA processing is coupled to RNA polymerase II (RNAPII) transcription through coordinated recruitment of accessory proteins to the Rpb1 C-terminal domain (CTD). Dynamic changes in CTD phosphorylation during transcription elongation are responsible for their recruitment, with serine 5 phosphorylation (S5-P) occurring toward the 5' end of genes and serine 2 phosphorylation (S2-P) occurring toward the Send. The proteins responsible for regulation of the transition state between S5-P and S2-P CTD remain elusive. We show that a conserved protein of unknown function, Rtr1, localizes within coding regions, with maximum levels of enrichment occurring between the peaks of S5-P and S2-P RNAPII Upon deletion of Rtr1, the S5-P form of RNAPII accumulates in both whole-cell extracts and throughout coding regions; additionally, RNAPII transcription is decreased, and termination defects are observed. Functional characterization of Rtr1 reveals its role as a CTD phosphatase essential for the S5-to-S2-P transition.

引用

页码：168 / 178

页数：11

共 47 条

[1] A role for the CPF 3′-end processing machinery in RNAP II-dependent gene looping [J].