Histone acetylation: a switch between repressive and permissive chromatin - Second in review series on chromatin dynamics

被引:712
作者
Eberharter, A [1 ]
Becker, PB [1 ]
机构
[1] Univ Munich, Adolf Butenandt Inst, D-80336 Munich, Germany
关键词
D O I
10.1093/embo-reports/kvf053
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
The organization of eukaryotic chromatin has a major impact on all nuclear processes involving DNA substrates. Gene expression is affected by the positioning of individual nucleosomes relative to regulatory sequence elements, by the folding of the nucleosomal fiber into higher-order structures and by the compartmentalization of functional domains within the nucleus. Because site-specific acetylation of nucleosomal histones influences all three aspects of chromatin organization, it is central to the switch between permissive and repressive chromatin structure. The targeting of enzymes that modulate the histone acetylation status of chromatin, in synergy with the effects mediated by other chromatin remodeling factors, is central to gene regulation.
引用
收藏
页码:224 / 229
页数:6
相关论文
共 74 条
[61]  
Turner BM, 2000, BIOESSAYS, V22, P836, DOI 10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.3.CO
[62]  
2-O
[63]   ATTACHMENT TO MOTHER AND BEHAVIOR WITH ADULTS IN PRESCHOOL [J].
TURNER, PJ .
BRITISH JOURNAL OF DEVELOPMENTAL PSYCHOLOGY, 1993, 11 :75-89
[64]   Transcriptional activators direct histone acetyltransferase complexes to nucleosomes [J].
Utley, RT ;
Ikeda, K ;
Grant, PA ;
Côté, J ;
Steger, DJ ;
Eberharter, A ;
John, S ;
Workman, JL .
NATURE, 1998, 394 (6692) :498-502
[65]   Physical association between the histone acetyl transferase CBP and a histone methyl transferase [J].
Vandel, L ;
Trouche, D .
EMBO REPORTS, 2001, 2 (01) :21-26
[66]   Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro [J].
VetteseDadey, M ;
Grant, PA ;
Hebbes, TR ;
CraneRobinson, C ;
Allis, CD ;
Workman, JL .
EMBO JOURNAL, 1996, 15 (10) :2508-2518
[67]   Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes [J].
Vignali, M ;
Steger, DJ ;
Neely, KE ;
Workman, JL .
EMBO JOURNAL, 2000, 19 (11) :2629-2640
[68]   Global histone acetylation and deacetylation in yeast [J].
Vogelauer, M ;
Wu, JS ;
Suka, N ;
Grunstein, M .
NATURE, 2000, 408 (6811) :495-498
[69]   Acetylation increases the α-helical content of the histone tails of the nucleosome [J].
Wang, XY ;
Moore, SC ;
Laszckzak, M ;
Ausió, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (45) :35013-35020
[70]   The bromodomain: a chromatin-targeting module? [J].
Winston, F ;
Allis, CD .
NATURE STRUCTURAL BIOLOGY, 1999, 6 (07) :601-604