Histone acetyltransferase complexes: one size doesn't fit all

被引：790

作者：

Lee, Kenneth K. ^{[1
]}

Workman, Jerry L. ^{[1
]}

机构：

[1] Stowers Inc, Kansas City, MO 64110 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2007年 / 8卷 / 04期

基金：

美国国家卫生研究院;

关键词：

NUCLEOTIDE EXCISION-REPAIR; DNA-DEPENDENT ACETYLATION; DROSOPHILA MSL COMPLEX; DOSAGE COMPENSATION; CHROMATIN-STRUCTURE; PROTEIN COMPLEX; SACCHAROMYCES-CEREVISIAE; SILENCING PROTEIN; DIVERSE FUNCTIONS; CRYSTAL-STRUCTURE;

D O I：

10.1038/nrm2145

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.

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收藏

页码：284 / 295

页数：12

相关论文

共 132 条

[1] Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila [J].

Akhtar, A ;

Becker, PB .

MOLECULAR CELL, 2000, 5 (02) :367-375

[2] Chromatin remodeling and the maintenance of genome integrity [J].

Allard, S ;

Masson, JY ;

Côté, J .

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 2004, 1677 (1-3) :158-164

[3] ACETYLATION + METHYLATION OF HISTONES + THEIR POSSIBLE ROLE IN REGULATION OF RNA SYNTHESIS [J].

ALLFREY, VG ;

FAULKNER, R ;

MIRSKY, AE .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1964, 51 (05) :786-+

[4] Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain [J].

Bannister, AJ ;

Zegerman, P ;

Partridge, JF ;

Miska, EA ;

Thomas, JO ;

Allshire, RC ;

Kouzarides, T .

NATURE, 2001, 410 (6824) :120-124

[5] Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair [J].

Bird, AW ;

Yu, DY ;

Pray-Grant, MG ;

Qiu, QF ;

Harmon, KE ;

Megee, PC ;

Grant, PA ;

Smith, MM ;

Christman, MF .

NATURE, 2002, 419 (6905) :411-415

[6] Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC [J].

Brand, M ;

Leurent, C ;

Mallouh, V ;

Tora, L ;

Schultz, P .

SCIENCE, 1999, 286 (5447) :2151-2153

[7] UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation [J].

Brand, M ;

Moggs, JG ;

Oulad-Abdelghani, M ;

Lejeune, F ;

Dilworth, FJ ;

Stevenin, J ;

Almouzni, G ;

Tora, L .

EMBO JOURNAL, 2001, 20 (12) :3187-3196

[8] Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation [J].

Brownell, JE ;

Zhou, JX ;

Ranalli, T ;

Kobayashi, R ;

Edmondson, DG ;

Roth, SY ;

Allis, CD .

CELL, 1996, 84 (06) :843-851

[9] Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation [J].

Brownell, JE ;

Allis, CD .

CURRENT OPINION IN GENETICS & DEVELOPMENT, 1996, 6 (02) :176-184

[10] AN ACTIVITY GEL ASSAY DETECTS A SINGLE, CATALYTICALLY ACTIVE HISTONE ACETYLTRANSFERASE SUBUNIT IN TETRAHYMENA MACRONUCLEI [J].

BROWNELL, JE ;

ALLIS, CD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (14) :6364-6368

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