TAFs与组蛋白八聚体异源四聚体核心之间的结构相似性。

Structural similarity between TAFs and the heterotetrameric core of the histone octamer.

作者信息

Xie X, Kokubo T, Cohen S L, Mirza U A, Hoffmann A, Chait B T, Roeder R G, Nakatani Y, Burley S K

机构信息

Laboratory of Molecular Biophysics, The Rockefeller University, New York, 10021, USA.

出版信息

Nature. 1996 Mar 28;380(6572):316-22. doi: 10.1038/380316a0.

DOI:10.1038/380316a0

PMID:8598927

Abstract

A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

摘要

以2.0埃的分辨率描述了一种由两个TFIID TATA盒结合蛋白相关因子（TA FII）组成的复合物。果蝇的dTAFII42和dTAFII62的氨基末端部分采用典型的组蛋白折叠结构，由一个长的中央α螺旋两侧的两个短α螺旋组成。与组蛋白H3和H4一样，dTAFII42和dTAFII62通过配对分子之间广泛的疏水接触形成紧密的异二聚体。在溶液和晶体状态下，dTAFII42/dTAFII62复合物以异四聚体形式存在，类似于组蛋白八聚体的（H3/H4）2异四聚体核心，这表明TFIID包含一个类似组蛋白八聚体的亚结构。