Structure and function of histone methylation binding proteins

被引:115
作者
Adams-Cioaba, Melanie A. [1 ]
Min, Jinrong [1 ,2 ]
机构
[1] Univ Toronto, Struct Genom Consortium, Toronto, ON M5G 1L6, Canada
[2] Univ Toronto, Dept Physiol, Toronto, ON M5S 1A8, Canada
关键词
chromatin remodeling; histone methylation; Tudor domain; MBT domain; PHD domain; PLANT HOMEODOMAIN FINGER; DE-NOVO METHYLATION; SMN TUDOR DOMAIN; PHD-FINGER; TUMOR-SUPPRESSOR; GENE-EXPRESSION; DROSOPHILA-MELANOGASTER; LYSINE METHYLATION; MOLECULAR-BASIS; POLYCOMB GROUP;
D O I
10.1139/O08-129
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
Chromatin structure is regulated by chromatin remodeling factors, histone exchange, linker histone association, and histone modification. Covalent modification of histones is an important factor in the regulation of the associated processes. The implementation and removal of various histone modifications have been implicated in DNA replication, repair, recombination, and transcription, and in RNA processing. In recent years, histone methylation has emerged as one of the key modifications regulating chromatin function. However, the mechanisms involved are complex and not well understood. A large volume of structural and biochemical information has been recently amassed for the Tudor, plant homeodomain (PHD), and malignant brain tumor (MBT) protein families. This review summarizes current knowledge of the structures and modes of recognition employed by the PHD, Tudor, and MBT domains in their interactions with target histone peptides.
引用
收藏
页码:93 / 105
页数:13
相关论文
共 99 条
  • [1] ACETYLATION + METHYLATION OF HISTONES + THEIR POSSIBLE ROLE IN REGULATION OF RNA SYNTHESIS
    ALLFREY, VG
    FAULKNER, R
    MIRSKY, AE
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1964, 51 (05) : 786 - +
  • [2] Phosphorylation and rapid relocalization of 53BP1 to nuclear foci upon DNA damage
    Anderson, L
    Henderson, C
    Adachi, Y
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (05) : 1719 - 1729
  • [3] Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    Bannister, AJ
    Zegerman, P
    Partridge, JF
    Miska, EA
    Thomas, JO
    Allshire, RC
    Kouzarides, T
    [J]. NATURE, 2001, 410 (6824) : 120 - 124
  • [4] Belenkaya TY, 2002, DEVELOPMENT, V129, P4089
  • [5] Covalent modifications of histones during development and disease pathogenesis
    Bhaumik, Sukesh R.
    Smith, Edwin
    Shilatifard, Ali
    [J]. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (11) : 1008 - 1016
  • [6] Bornemann D, 1998, GENETICS, V150, P675
  • [7] TUDOR, A GENE REQUIRED FOR ASSEMBLY OF THE GERM PLASM IN DROSOPHILA-MELANOGASTER
    BOSWELL, RE
    MAHOWALD, AP
    [J]. CELL, 1985, 43 (01) : 97 - 104
  • [8] Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    Botuyan, Maria Victoria
    Lee, Joseph
    Ward, Irene M.
    Kim, Ja-Eun
    Thompson, James R.
    Chen, Junjie
    Mer, Georges
    [J]. CELL, 2006, 127 (07) : 1361 - 1373
  • [9] Dnmt3L and the establishment of maternal genomic imprints
    Bourc'his, D
    Xu, GL
    Lin, CS
    Bollman, B
    Bestor, TH
    [J]. SCIENCE, 2001, 294 (5551) : 2536 - 2539
  • [10] Meiotic catastrophe and retrotransposon reactivation in male germ cells lacking Dnmt3L
    Bourc'his, D
    Bestor, TH
    [J]. NATURE, 2004, 431 (7004) : 96 - 99