A MULTISUBUNIT COMPLEX-ASSOCIATED WITH THE RNA POLYMERASE-II CTD AND TATA-BINDING PROTEIN IN YEAST

被引：406

作者：

THOMPSON, CM ^{[1
]}

KOLESKE, AJ ^{[1
]}

CHAO, DM ^{[1
]}

YOUNG, RA ^{[1
]}

机构：

[1] MIT, DEPT BIOL, CAMBRIDGE, MA 02139 USA

来源：

CELL | 1993年 / 73卷 / 07期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0092-8674(93)90362-T

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：

We report genetic and biochemical evidence that the RNA polymerase II carboxy-terminal domain (CTD) interacts with a large multisubunit complex that contains TATA-binding protein (TBP) and is an integral part of the transcription initiation complex. The isolation and characterization of extragenic suppressors of S. cerevisiae RNA polymerase II CTD truncation mutations led us to identify SRB2, SRB4, SRB5, and SRB6 as genes involved in CTD function in vivo. SRB2 was previously isolated and shown to encode a 23 kd TBP-binding protein. The four SRB proteins and a portion of cellular TBP are components of a high molecular weight multisubunit complex that is tightly bound to RNA polymerase II. This SRB-TBP complex binds specifically to recombinant CTD protein. In vitro transcription and template commitment assays confirm that SRB2 and SRB5 are components of a functional preinitiation complex and are required for efficient transcription initiation.

引用

页码：1361 / 1375

页数：15

共 80 条

[71]

THOMPSON NE, 1989, J BIOL CHEM, V264, P11511

[72] THE MAMMALIAN TFIID PROTEIN IS PRESENT IN 2 FUNCTIONALLY DISTINCT COMPLEXES [J].