Phylogenomics of the nucleosome

被引:412
作者
Malik, HS
Henikoff, S [1 ]
机构
[1] Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA
[2] Fred Hutchinson Canc Res Ctr, Howard Hughes Med Inst, Seattle, WA 98109 USA
关键词
D O I
10.1038/nsb996
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
Histones are best known as the architectural proteins that package the DNA of eukaryotic organisms, forming octameric nucleosome cores that the double helix wraps tightly around. Although histones have traditionally been viewed as slowly evolving scaffold proteins that lack diversification beyond their abundant tail modifications, recent studies have revealed that variant histones have evolved for diverse functions. H2A and H3 variants have diversified to assume roles in epigenetic silencing, gene expression and centromere function. Such diversification of histone variants and deviants contradicts the perception of histones as monotonous members of multigene families that indiscriminately package and compact the genome. How these diverse functions have evolved from ancestral forms can be addressed by applying phylogenetic tools to increasingly abundant sequence data.
引用
收藏
页码:882 / 891
页数:10
相关论文
共 70 条
  • [1] The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
    Ahmad, K
    Henikoff, S
    [J]. MOLECULAR CELL, 2002, 9 (06) : 1191 - 1200
  • [2] ALLIS CD, 1986, J BIOL CHEM, V261, P1941
  • [3] The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    Angelov, D
    Molla, A
    Perche, PY
    Hans, F
    Côté, J
    Khochbin, S
    Bouvet, P
    Dimitrov, S
    [J]. MOLECULAR CELL, 2003, 11 (04) : 1033 - 1041
  • [4] THE NUCLEOSOMAL CORE HISTONE OCTAMER AT 3.1-A RESOLUTION - A TRIPARTITE PROTEIN ASSEMBLY AND A LEFT-HANDED SUPERHELIX
    ARENTS, G
    BURLINGAME, RW
    WANG, BC
    LOVE, WE
    MOUDRIANAKIS, EN
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (22) : 10148 - 10152
  • [6] Histone H1 and evolution of sperm nuclear basic proteins
    Ausió, J
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (44) : 31115 - 31118
  • [7] BOSCH A, 1995, EUR J CELL BIOL, V68, P220
  • [8] Cell division -: A histone-H3-like protein in C-elegans
    Buchwitz, BJ
    Ahmad, K
    Moore, LL
    Roth, MB
    Henikoff, S
    [J]. NATURE, 1999, 401 (6753) : 547 - 548
  • [9] Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks
    Celeste, A
    Fernandez-Capetillo, O
    Kruhlak, MJ
    Pilch, DR
    Staudt, DW
    Lee, A
    Bonner, RF
    Bonner, WM
    Nussenzweig, A
    [J]. NATURE CELL BIOLOGY, 2003, 5 (07) : 675 - U51
  • [10] A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    Chadwick, BP
    Willard, HF
    [J]. JOURNAL OF CELL BIOLOGY, 2001, 152 (02) : 375 - 384