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

Xiaoling Xie; Tetsuro Kokubo; Steven L. Cohen; Urooj A. Mirza; Alexander Hoffmann; Brian T. Chait; Robert G. Roeder; Yoshihiro Nakatani; Stephen K. Burley

doi:10.1038/380316a0

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

Xiaoling Xie, Tetsuro Kokubo, Steven L. Cohen, Urooj A. Mirza, Alexander Hoffmann, Brian T. Chait, Robert G. Roeder, Yoshihiro Nakatani, Stephen K. Burley

Research output: Contribution to journal › Review article › peer-review

228 Scopus citations

Abstract

A complex of two TFIID TATA box-binding protein-associated factors (TAF(II)s) is described at 2.0 Å resolution. The amino-terminal portions of dTAF(II)42 and dTAF(II)62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAF(II)42 and dTAF(II)62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAF(II)42/dTAF(II)62 complex exists as a heterotetramer, resembling the (H3/H4), heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

Original language	English (US)
Pages (from-to)	316-322
Number of pages	7
Journal	Nature
Volume	380
Issue number	6572
DOIs	https://doi.org/10.1038/380316a0
State	Published - Mar 28 1996
Externally published	Yes

All Science Journal Classification (ASJC) codes

General

Access to Document

10.1038/380316a0

Cite this

@article{a96c6b044d024e41948f57121d7bbfc3,

title = "Structural similarity between TAFs and the heterotetrameric core of the histone octamer",

abstract = "A complex of two TFIID TATA box-binding protein-associated factors (TAF(II)s) is described at 2.0 {\AA} resolution. The amino-terminal portions of dTAF(II)42 and dTAF(II)62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAF(II)42 and dTAF(II)62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAF(II)42/dTAF(II)62 complex exists as a heterotetramer, resembling the (H3/H4), heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.",

author = "Xiaoling Xie and Tetsuro Kokubo and Cohen, {Steven L.} and Mirza, {Urooj A.} and Alexander Hoffmann and Chait, {Brian T.} and Roeder, {Robert G.} and Yoshihiro Nakatani and Burley, {Stephen K.}",

year = "1996",

month = mar,

day = "28",

doi = "10.1038/380316a0",

language = "English (US)",

volume = "380",

pages = "316--322",

journal = "Nature",

issn = "0028-0836",

publisher = "Nature Publishing Group",

number = "6572",

}

TY - JOUR

T1 - Structural similarity between TAFs and the heterotetrameric core of the histone octamer

AU - Xie, Xiaoling

AU - Kokubo, Tetsuro

AU - Cohen, Steven L.

AU - Mirza, Urooj A.

AU - Hoffmann, Alexander

AU - Chait, Brian T.

AU - Roeder, Robert G.

AU - Nakatani, Yoshihiro

AU - Burley, Stephen K.

PY - 1996/3/28

Y1 - 1996/3/28

N2 - A complex of two TFIID TATA box-binding protein-associated factors (TAF(II)s) is described at 2.0 Å resolution. The amino-terminal portions of dTAF(II)42 and dTAF(II)62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAF(II)42 and dTAF(II)62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAF(II)42/dTAF(II)62 complex exists as a heterotetramer, resembling the (H3/H4), heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

AB - A complex of two TFIID TATA box-binding protein-associated factors (TAF(II)s) is described at 2.0 Å resolution. The amino-terminal portions of dTAF(II)42 and dTAF(II)62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAF(II)42 and dTAF(II)62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAF(II)42/dTAF(II)62 complex exists as a heterotetramer, resembling the (H3/H4), heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

UR - http://www.scopus.com/inward/record.url?scp=0029869460&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029869460&partnerID=8YFLogxK

U2 - 10.1038/380316a0

DO - 10.1038/380316a0

M3 - Review article

C2 - 8598927

AN - SCOPUS:0029869460

SN - 0028-0836

VL - 380

SP - 316

EP - 322

JO - Nature

JF - Nature

IS - 6572

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this