Characterization of the residues phosphorylated in vitro by different C-terminal domain kinases

被引:105
作者
Trigon, S
Serizawa, H
Conaway, JW
Conaway, RC
Jackson, SP
Morange, M
机构
[1] ENS, Unite Genet Mol, F-75230 Paris 05, France
[2] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA
[3] Oklahoma Med Res Fdn, Oklahoma City, OK 73104 USA
[4] Wellcome Canc Res Campaign Inst, Cambridge CB2 1QR, England
关键词
D O I
10.1074/jbc.273.12.6769
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 C-terminal part of the largest subunit of eukaryotic RNA polymerase II is composed solely of the highly repeated consensus sequence Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7). This domain, called the C-terminal domain (CTD), is phosphorylated mostly at serine residues during transcription initiation, but the precise role of this phosphorylation remains controversial, Several protein kinases are able to phosphorylate this sequence in vitro, The aim of this work was to define the positions of the amino acids phosphorylated by four of these CTD kinases (transcription factor (TF) IIH-kinase, DNA-dependent protein kinase, and the mitogen-activated protein kinases ERK1 and ERK2) and to compare the specificity of these different protein kinases, We show that TFIIH kinase and the mitogen-activated protein kinases phosphorylate only serine 5 of the CTD sequence, whereas DNA-dependent protein kinase phosphorylates serines 2 and 7, Among the different CTD kinases, only TFIIH kinase is appreciably more active on two repeats of the consensus sequence than on one motif, These in vitro results can provide some clues to the nature of the protein kinases responsible for the in vivo phosphorylation of the RNA polymerase CTD. In particular, the ratio of phosphorylated serine to threonine observed in vivo cannot be explained if TFIIH kinase is the only protein kinase involved in the phosphorylation of the CTD.
引用
收藏
页码:6769 / 6775
页数:7
相关论文
共 69 条
[1]   MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH [J].
Adamczewski, JP ;
Rossignol, M ;
Tassan, JP ;
Nigg, EA ;
Moncollin, V ;
Egly, JM .
EMBO JOURNAL, 1996, 15 (08) :1877-1884
[2]   THE C-TERMINAL DOMAIN OF THE LARGEST SUBUNIT OF RNA POLYMERASE-II OF SACCHAROMYCES-CEREVISIAE, DROSOPHILA-MELANOGASTER, AND MAMMALS - A CONSERVED STRUCTURE WITH AN ESSENTIAL FUNCTION [J].
ALLISON, LA ;
WONG, JKC ;
FITZPATRICK, VD ;
MOYLE, M ;
INGLES, CJ .
MOLECULAR AND CELLULAR BIOLOGY, 1988, 8 (01) :321-329
[3]   EXTENSIVE HOMOLOGY AMONG THE LARGEST SUBUNITS OF EUKARYOTIC AND PROKARYOTIC RNA-POLYMERASES [J].
ALLISON, LA ;
MOYLE, M ;
SHALES, M ;
INGLES, CJ .
CELL, 1985, 42 (02) :599-610
[4]  
ALVAREZ E, 1991, J BIOL CHEM, V266, P15277
[5]  
Anderson Carl W., 1992, Critical Reviews in Eukaryotic Gene Expression, V2, P283
[6]  
ARIAS JA, 1991, J BIOL CHEM, V266, P8055
[7]   C-JUN IS PHOSPHORYLATED BY THE DNA-DEPENDENT PROTEIN-KINASE INVITRO - DEFINITION OF THE MINIMAL KINASE RECOGNITION MOTIF [J].
BANNISTER, AJ ;
GOTTLIEB, TM ;
KOUZARIDES, T ;
JACKSON, SP .
NUCLEIC ACIDS RESEARCH, 1993, 21 (05) :1289-1295
[8]   TYROSINE PHOSPHORYLATION OF MAMMALIAN RNA POLYMERASE-II CARBOXYL-TERMINAL DOMAIN [J].
BASKARAN, R ;
DAHMUS, ME ;
WANG, JYJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (23) :11167-11171
[9]   PRESENCE OF PHOSPHORYLATED SUBUNITS IN YEAST RNA POLYMERASES-A AND POLYMERASES-B [J].
BUHLER, JM ;
IBORRA, F ;
SENTENAC, A ;
FROMAGEOT, P .
FEBS LETTERS, 1976, 71 (01) :37-41
[10]  
CADENA DL, 1987, J BIOL CHEM, V262, P12468