An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S-cerevisiae

被引:171
作者
Kobor, MS
Archambault, J
Lester, W
Holstege, FCP
Gileadi, O
Jansma, DB
Jennings, EG
Kouyoumdjian, F
Davidson, AR
Young, RA
Greenblatt, J
机构
[1] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada
[2] Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5G 1L6, Canada
[3] Boehringer Ingelheim Canada Ltd, Dept Biol Sci, Biomega Res Div, Laval, PQ H7S 2G5, Canada
[4] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA
[5] MIT, Dept Biol, Cambridge, MA 02139 USA
[6] Weizmann Inst Sci, Dept Mol Genet, IL-76100 Rehovot, Israel
关键词
D O I
10.1016/S1097-2765(00)80187-2
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
The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, Psi Psi Psi DXDX(T/V)Psi Psi, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.
引用
收藏
页码:55 / 62
页数:8
相关论文
共 31 条
[1]   Broad, but not universal, transcriptional requirement for yTAFII17, a histone H3-like TAFII present in TFIID and SAGA [J].
Apone, LM ;
Virbasius, CA ;
Holstege, FCP ;
Wang, J ;
Young, RA ;
Green, MR .
MOLECULAR CELL, 1998, 2 (05) :653-661
[2]  
Archambault J, 1996, GENETICS, V142, P737
[3]   FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO [J].
Archambault, J ;
Pan, GH ;
Dahmus, GK ;
Cartier, M ;
Marshall, N ;
Zhang, S ;
Dahmus, ME ;
Greenblatt, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (42) :27593-27601
[4]   An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae [J].
Archambault, J ;
Chambers, RS ;
Kobor, MS ;
Ho, Y ;
Cartier, M ;
Bolotin, D ;
Andrews, B ;
Kane, CM ;
Greenblatt, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (26) :14300-14305
[5]  
Ausubel F.A., 1997, CURRENT PROTOCOLS MO, DOI DOI 10.1.4
[6]   The structure and mechanism of protein phosphatases: Insights into catalysis and regulation [J].
Barford, D ;
Das, AK ;
Egloff, MP .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1998, 27 :133-164
[7]   REGULATION OF TRANSCRIPTIONAL ELONGATION BY RNA-POLYMERASE-II [J].
BENTLEY, DL .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 1995, 5 (02) :210-216
[8]  
CADENA DL, 1987, J BIOL CHEM, V262, P12468
[9]   Purification and characterization of an RNA polymerase II phosphatase from yeast [J].
Chambers, RS ;
Kane, CM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (40) :24498-24504
[10]   THE ACTIVITY OF COOH-TERMINAL DOMAIN PHOSPHATASE IS REGULATED BY A DOCKING SITE ON RNA-POLYMERASE-II AND BY THE GENERAL TRANSCRIPTION FACTORS IIF AND IIB [J].
CHAMBERS, RS ;
WANG, BQ ;
BURTON, ZF ;
DAHMUS, ME .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (25) :14962-14969