Structure of histone deacetylases: Insights into substrate recognition and catalysis

被引:75
作者
Marmorstein, R [1 ]
机构
[1] Univ Penn, Wistar Inst, Philadelphia, PA 19104 USA
[2] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA
关键词
D O I
10.1016/S0969-2126(01)00690-6
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 deacetylases catalyze the removal of the acetyl moiety from acetyl-lysine within histories to promote gene repression and silencing. These enzymes fall into distinct families based on primary sequence homology and functional properties in vivo. Recent structural studies of histone deacetylases and their homologs from bacteria have provided important insights into the mode of substrate recognition and catalysis by these enzymes.
引用
收藏
页码:1127 / 1133
页数:7
相关论文
共 45 条
[21]   A role for histone deacetylase activity in HDAC1-mediated transcriptional repression [J].
Hassig, CA ;
Tong, JK ;
Fleischer, TC ;
Owa, T ;
Grable, PG ;
Ayer, DE ;
Schreiber, SL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (07) :3519-3524
[22]   Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase [J].
Imai, S ;
Armstrong, CM ;
Kaeberlein, M ;
Guarente, L .
NATURE, 2000, 403 (6771) :795-800
[23]   Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo [J].
Kadosh, D ;
Struhl, K .
GENES & DEVELOPMENT, 1998, 12 (06) :797-805
[24]   Structure of a unique binuclear manganese cluster in arginase [J].
Kanyo, ZF ;
Scolnick, LR ;
Ash, DE ;
Christianson, DW .
NATURE, 1996, 383 (6600) :554-557
[25]   Sin meets NuRD and other tails of repression [J].
Knoepfler, PS ;
Eisenman, RN .
CELL, 1999, 99 (05) :447-450
[26]   The silencing protein SIR2 and its homologs are MAD-dependent protein deacetylases [J].
Landry, J ;
Sutton, A ;
Tafrov, ST ;
Heller, RC ;
Stebbins, J ;
Pillus, L ;
Sternglanz, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (11) :5807-5811
[27]   Role of the histone deacetylase complex in acute promyelocytic leukaemia [J].
Lin, RJ ;
Nagy, L ;
Inoue, S ;
Shao, WL ;
Miller, WH ;
Evans, RM .
NATURE, 1998, 391 (6669) :811-814
[28]   Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation [J].
McKinsey, TA ;
Zhang, CL ;
Lu, JR ;
Olson, EN .
NATURE, 2000, 408 (6808) :106-111
[29]   Crystal structure of a SIR2 homolog-NAD complex [J].
Min, JR ;
Landry, J ;
Sternglanz, R ;
Xu, RM .
CELL, 2001, 105 (02) :269-279
[30]   The TAF(II)250 subunit of TFIID has histone acetyltransferase activity [J].
Mizzen, CA ;
Yang, XJ ;
Kokubo, T ;
Brownell, JE ;
Bannister, AJ ;
OwenHughes, T ;
Workman, J ;
Wang, L ;
Berger, SL ;
Kouzarides, T ;
Nakatani, Y ;
Allis, CD .
CELL, 1996, 87 (07) :1261-1270