The histone fold is a key structural motif of transcription factor TFIID

被引：111

作者：

Gangloff, YG ^{[1
]}

Romier, C ^{[1
]}

Thuault, S ^{[1
]}

Werten, S ^{[1
]}

Davidson, I ^{[1
]}

机构：

[1] ULP, CNRS, INSERM, CU Strasbourg,Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2001年 / 26卷 / 04期

关键词：

D O I：

10.1016/S0968-0004(00)01741-2

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：

Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex.

引用

页码：250 / 257

页数：8

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