The human histone deacetylase family

被引:481
作者
Gray, SG
Ekström, TJ
机构
[1] Karolinska Hosp, Ctr Mol Med, Lab Mol Dev & Tumor Biol, S-17176 Stockholm, Sweden
[2] VanAndel Res Inst, Grand Rapids, MI 49503 USA
关键词
HDAC; RPD3; HDA1; Sir2;
D O I
10.1006/excr.2000.5080
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Since the identification of the first histone deacetylase (Taunton et at, Science 272, 408-411), several new members have been isolated. They can loosely be separated into entities on the basis of their similarity to various yeast histone deacetylases. The first class is represented by its closeness to the yeast Rpd3-like proteins, and the second most recently discovered class has similarities to yeast Hda1-like proteins. However, due to the fact that several different research groups isolated the Hda1-like histone deacetylases independently, there have been various different nomenclatures used to describe the various members, which can lead to confusion in the interpretation of this family's functions and interactions. With the discovery of another novel murine histone deacetylase, homologous to yeast Sir2, the number of members of this family is set to increase, as 7 human homologues of this gene have been isolated. In the light of these recent discoveries, we have examined the literature data and conducted a database analysis of the isolated histone deacetylases and potential candidates. The results obtained suggest that the number of; histone deacetylases within the human genome may be as high as 17 and are discussed in relation to their homology to the yeast histone deacetylases. (C) 2001 Academic Press.
引用
收藏
页码:75 / 83
页数:9
相关论文
共 104 条
[1]   Post-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometry [J].
Abraham, J ;
Kelly, J ;
Thibault, P ;
Benchimol, S .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 295 (04) :853-864
[2]   Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2 [J].
Afshar, G ;
Murnane, JP .
GENE, 1999, 234 (01) :161-168
[3]   Ikaros sets thresholds for T cell activation and regulates chromosome propagation [J].
Avitahl, N ;
Winandy, S ;
Friedrich, C ;
Jones, B ;
Ge, YM ;
Georgopoulos, K .
IMMUNITY, 1999, 10 (03) :333-343
[4]   RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex [J].
Bach, I ;
Rodriguez-Esteban, C ;
Carrière, C ;
Bhushan, A ;
Krones, A ;
Rose, DW ;
Glass, CK ;
Andersen, B ;
Belmonte, JCI ;
Rosenfeld, MG .
NATURE GENETICS, 1999, 22 (04) :394-399
[5]   Acetylation of importin-α nuclear import factors by CBP/p300 [J].
Bannister, AJ ;
Miska, EA ;
Görlich, D ;
Kouzarides, T .
CURRENT BIOLOGY, 2000, 10 (08) :467-470
[6]   Identification of mouse histone deacetylase 1 as a growth factor-inducible gene [J].
Bartl, S ;
Taplick, J ;
Lagger, G ;
Khier, H ;
Kuchler, K ;
Seiser, C .
MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (09) :5033-5043
[7]   Gene silencing - Methylation meets acetylation [J].
Bestor, TH .
NATURE, 1998, 393 (6683) :311-312
[8]   Human histone deacetylase 2, HDAC2 (human RPD3), is localized to 6q21 by radiation hybrid mapping [J].
Betz, R ;
Gray, SG ;
Ekström, C ;
Larsson, C ;
Ekström, TJ .
GENOMICS, 1998, 52 (02) :245-246
[9]   β-catenin-histone deacetylase interactions regulate the transition of LEF1 from a transcriptional repressor to an activator [J].
Billin, AN ;
Thirlwell, H ;
Ayer, DE .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (18) :6882-6890
[10]   Retinoblastoma protein recruits histone deacetylase to repress transcription [J].
Brehm, A ;
Miska, EA ;
McCance, DJ ;
Reid, JL ;
Bannister, AJ ;
Kouzarides, T .
NATURE, 1998, 391 (6667) :597-601