A kinetic model for the early steps of RNA synthesis by human RNA polymerase II

被引:33
作者
Kugel, JF [1 ]
Goodrich, JA [1 ]
机构
[1] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80309 USA
关键词
D O I
10.1074/jbc.M006401200
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
Eukaryotic mRNA synthesis is a highly regulated process involving numerous proteins acting in concert with RNA polymerase II to set levels of transcription from individual promoters. The transcription reaction consists of multiple steps beginning with preinitiation complex formation and ending in the production of a full-length primary transcript. We used pre-steady-state approaches to study the steps of human mRNA transcription at the adenovirus major late promoter in a minimal in vitro transcription system. These kinetic studies revealed an early transition in RNA polymerase II transcription, termed escape commitment, that occurs after initiation and prior to promoter escape. Escape commitment is rapid and is characterized by sensitivity to competitor DNA. Upon completion of escape commitment, ternary complexes are resistant to challenge by competitor DNA and slowly proceed forward through promoter escape. Escape commitment is stimulated by transcription factors TFIIE and TFIIH. We measured forward and reverse rate constants for discrete steps in transcription and present a kinetic model for the mechanism of RNA polymerase II transcription that describes five distinct steps (preinitiation complex formation, initiation, escape commitment, promoter escape, and transcript elongation) and clearly shows promoter escape is rate-limiting in this system.
引用
收藏
页码:40483 / 40491
页数:9
相关论文
共 38 条
[1]  
BORUKHOV S, 1993, J BIOL CHEM, V268, P23477
[2]   Distinct roles for the helicases of TFIIH in transcript initiation and promoter escape [J].
Bradsher, J ;
Coin, F ;
Egly, JM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (04) :2532-2538
[3]   5 INTERMEDIATE COMPLEXES IN TRANSCRIPTION INITIATION BY RNA POLYMERASE-II [J].
BURATOWSKI, S ;
HAHN, S ;
GUARENTE, L ;
SHARP, PA .
CELL, 1989, 56 (04) :549-561
[4]  
CAI H, 1987, J BIOL CHEM, V262, P298
[5]   Structure of a transcribing T7 RNA polymerase initiation complex [J].
Cheetham, GMT ;
Steitz, TA .
SCIENCE, 1999, 286 (5448) :2305-2309
[6]   Architecture of RNA polymerase II and implications for the transcription mechanism [J].
Cramer, P ;
Bushnell, DA ;
Fu, JH ;
Gnatt, AL ;
Maier-Davis, B ;
Thompson, NE ;
Burgess, RR ;
Edwards, AM ;
David, PR ;
Kornberg, RD .
SCIENCE, 2000, 288 (5466) :640-649
[7]   DUAL ROLE OF TFIIH IN DNA EXCISION-REPAIR AND IN TRANSCRIPTION BY RNA-POLYMERASE-II [J].
DRAPKIN, R ;
REARDON, JT ;
ANSARI, A ;
HUANG, JC ;
ZAWEL, L ;
AHN, KJ ;
SANCAR, A ;
REINBERG, D .
NATURE, 1994, 368 (6473) :769-772
[8]   Promoter escape by RNA polymerase II - A role for an ATP cofactor in suppression of arrest by polymerase at promoter-proximal sites [J].
Dvir, A ;
Conaway, RC ;
Conaway, JW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (38) :23352-23356
[9]   Promoter escape by RNA polymerase II - Formation of an escape-competent transcriptional, intermediate is a prerequisite for exit of polymerase from the promoter [J].
Dvir, A ;
Tan, SY ;
Conaway, JW ;
Conaway, RC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (45) :28175-28178
[10]   A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes [J].
Dvir, A ;
Conaway, RC ;
Conaway, JW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (17) :9006-9010