Patterning chromatin: form and function for H2A.Z variant nucleosomes

被引:82
作者
Raisner, RM [1 ]
Madhani, HD [1 ]
机构
[1] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/j.gde.2006.02.005
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Although many histone variants are specific to higher eukaryotes, the H2A variant H2A.Z has been conserved during eukaryotic evolution. Genetic studies have demonstrated roles for H2A.Z in antagonizing gene-silencing, chromosome stability and gene activation. Biochemical work has identified a conserved chromatin-remodeling complex responsible for H2A.Z deposition. Recent studies have shown that two H2A.Z nucleosomes flank a nucleosome-free region containing the transcription initiation site in promoters of both active and inactive genes in Saccharomyces cerevisiae. This chromatin pattern is generated through the action of a DNA deposition signal and a specific pattern of histone tail acetylation.
引用
收藏
页码:119 / 124
页数:6
相关论文
共 38 条
[1]   Characterization of the stability and folding of H2A.Z chromatin particles -: Implications for transcriptional activation [J].
Abbott, DW ;
Ivanova, VS ;
Wang, XY ;
Bonner, WM ;
Ausió, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (45) :41945-41949
[2]   H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions [J].
Adam, M ;
Robert, F ;
Larochelle, M ;
Gaudreau, L .
MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (18) :6270-6279
[3]  
ALLIS CD, 1986, J BIOL CHEM, V261, P1941
[4]   The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken [J].
Bruce, K ;
Myers, FA ;
Mantouvalou, E ;
Lefevre, P ;
Greaves, I ;
Bonifer, C ;
Tremethick, DJ ;
Thorne, AW ;
Crane-Robinson, C .
NUCLEIC ACIDS RESEARCH, 2005, 33 (17) :5633-5639
[5]   The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes [J].
Cai, Y ;
Jin, JJ ;
Florens, L ;
Swanson, SK ;
Kusch, T ;
Li, B ;
Workman, JL ;
Washburn, MP ;
Conaway, RC ;
Conaway, JW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (14) :13665-13670
[6]   ANALYSIS OF A HISTONE H2A VARIANT FROM FISSION YEAST - EVIDENCE FOR A ROLE IN CHROMOSOME STABILITY [J].
CARR, AM ;
DORRINGTON, SM ;
HINDLEY, J ;
PHEAR, GA ;
AVES, SJ ;
NURSE, P .
MOLECULAR AND GENERAL GENETICS, 1994, 245 (05) :628-635
[7]   Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals [J].
Costanzi, C ;
Pehrson, JR .
NATURE, 1998, 393 (6685) :599-601
[8]   H2A.Z functions to regulate progression through the cell cycle [J].
Dhillon, N ;
Oki, M ;
Szyjka, SJ ;
Aparicio, OM ;
Kamakaka, RT .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (02) :489-501
[9]   CHARACTERIZATION OF A CDNA CLONE CODING FOR A SEA-URCHIN HISTONE H2A VARIANT RELATED TO THE H2A.F/Z HISTONE PROTEIN IN VERTEBRATES [J].
ERNST, SG ;
MILLER, H ;
BRENNER, CA ;
NOCENTEMCGRATH, C ;
FRANCIS, S ;
MCISAAC, R .
NUCLEIC ACIDS RESEARCH, 1987, 15 (11) :4629-4644
[10]   Histone variant H2A.Z is required for early mammalian development [J].
Faast, R ;
Thonglairoam, V ;
Schulz, TC ;
Beall, J ;
Wells, JRE ;
Taylor, H ;
Matthaei, K ;
Rathjen, PD ;
Tremethick, DJ ;
Lyons, I .
CURRENT BIOLOGY, 2001, 11 (15) :1183-1187