Three-dimensional structure of the human TFIID-IIA-IIB complex

被引：112

作者：

Andel, F

Ladurner, AG

Inouye, C

Tjian, R

Nogales, E ^{[1
]}

机构：

[1] Univ Calif Berkeley, Lawrence Berkeley Lab, Div Life Sci, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Mol & Cellular Biol, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA

来源：

SCIENCE | 1999年 / 286卷 / 5447期

关键词：

D O I：

10.1126/science.286.5447.2153

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The multisubunit transcription factor IID (TFIID) is an essential component of the eukaryotic RNA polymerase II machinery that works in concert with TFIIA (IIA) and TFIIB (IIB) to assemble initiation complexes at core eukaryotic promoters. Here the structures of human TFIID and the TFIID-IIA-IIB complex that were obtained by electron microscopy and image analysis to 35 angstrom resolution are presented. TFIID is a trilobed, horseshoe-shaped structure, with TFIIA and TFIIB bound on opposite Lobes and flanking a central cavity. Antibody studies Locate the TATA-binding protein (TBP) between TFIIA and TFIIB at the top of the cavity that most Likely encompasses the TATA DNA binding region of the supramolecular complex.

引用

页码：2153 / 2156

页数：4

共 47 条

[1] Cyclin D1 associates with the TBP-associated factor TAFII250 to regulate Sp1-mediated transcription [J].