Histone modifying enzymes: Structures, mechanisms, and specificities

被引:221
作者
Marmorstein, Ronen [2 ,3 ]
Trievel, Raymond C. [1 ]
机构
[1] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA
[2] Wistar Inst Anat & Biol, Program Gene Express & Regulat, Philadelphia, PA 19104 USA
[3] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS | 2009年 / 1789卷 / 01期
基金
美国国家卫生研究院;
关键词
Chromatin; Transcription; Histone modification; Histone acetyltransferase; Histone demethylase; CATALYTIC MECHANISM; ANDROGEN-RECEPTOR; JMJD2; FAMILY; RAT-LIVER; H3; ACETYLTRANSFERASE; PROTEIN; DEMETHYLASE; GENE; ACETYLATION;
D O I
10.1016/j.bbagrm.2008.07.009
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
Histone modifying enzymes catalyze the addition or removal of an array of covalent modifications in histone and non-histone proteins. Within the context of chromatin, these modifications regulate gene expression as well as other genomic functions and have been implicated in establishing and maintaining a heritable epigenetic code that contributes to defining cell identity and fate. Biochemical and structural characterization of histone modifying enzymes has yielded important insights into their respective catalytic mechanisms, substrate specificities, and regulation. In this review, we summarize recent advances in understanding these enzymes, highlighting studies of the histone acetyltransferases (HATS) p300 (also now known as KAT3B) and Rtt109 (KAT11) and the histone lysine demethylases (HDMs) LSD1 (KDM1) and JMJD2A (KDM4A), present overriding themes that derive from these studies, and pose remaining questions concerning their regulatory roles in mediating DNA transactions. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:58 / 68
页数:11
相关论文
共 107 条
[21]   The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing [J].
De Santa, Francesca ;
Totaro, Maria Grazia ;
Prosperini, Elena ;
Notarbartolo, Samuele ;
Testa, Giuseppe ;
Natoli, Gioacchino .
CELL, 2007, 130 (06) :1083-1094
[22]   Circadian regulator CLOCK is a histone acetyltransferase [J].
Doi, Masao ;
Hirayama, Jun ;
Sassone-Corsi, Paolo .
CELL, 2006, 125 (03) :497-508
[23]   Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56 [J].
Driscoll, Robert ;
Hudson, Amanda ;
Jackson, Stephen P. .
SCIENCE, 2007, 315 (5812) :649-652
[24]   The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase [J].
Eissenberg, Joel C. ;
Lee, Min Gyu ;
Schneider, Jessica ;
Ilvarsonn, Anne ;
Shiekhattar, Ramin ;
Shilatifard, Ali .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (04) :344-346
[25]   Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing [J].
Emre, NCT ;
Ingvarsdottir, K ;
Wyce, A ;
Wood, A ;
Krogan, NJ ;
Henry, KW ;
Li, KQ ;
Marmorstein, R ;
Greenblatt, JF ;
Shilatifard, A ;
Berger, SL .
MOLECULAR CELL, 2005, 17 (04) :585-594
[26]   ASF1 binds to a heterodimer of histories H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA [J].
English, CM ;
Maluf, NK ;
Tripet, B ;
Churchill, MEA ;
Tyler, JK .
BIOCHEMISTRY, 2005, 44 (42) :13673-13682
[27]   Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells [J].
Fodor, Barna D. ;
Kubicek, Stefan ;
Yonezawa, Masato ;
O'Sullivan, Roderick J. ;
Sengupta, Roopsha ;
Perez-Burgos, Laura ;
Opravil, Susanne ;
Mechtler, Karl ;
Schotta, Gunnar ;
Jenuwein, Thomas .
GENES & DEVELOPMENT, 2006, 20 (12) :1557-1562
[28]   Human histone demethylase LSD1 reads the histone code [J].
Forneris, F ;
Binda, C ;
Vanoni, MA ;
Battaglioli, E ;
Mattevi, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (50) :41360-41365
[29]   Structural basis of LSD1-CoREST selectivity in histone H3 recognition [J].
Forneris, Federico ;
Binda, Claudia ;
Adamo, Antonio ;
Battaglioli, Elena ;
Mattevi, Andrea .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (28) :20070-20074
[30]   A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1 [J].
Forneris, Federico ;
Binda, Claudia ;
Dall'Aglio, Annachiara ;
Fraaije, Marco W. ;
Battaglioli, Elena ;
Mattevi, Andrea .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (46) :35289-35295