Components of the DNA methylation system of chromatin control are RNA-binding proteins

被引:127
作者
Jeffery, L [1 ]
Nakielny, S [1 ]
机构
[1] Canc Res UK, London Res Inst, Lincolns Inn Fields Labs, London WC2A 3PX, England
关键词
D O I
10.1074/jbc.M409070200
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
The view that autosomal gene expression is controlled exclusively by protein trans-acting factors has been challenged recently by the identification of RNA molecules that regulate chromatin. In the majority of cases where RNA molecules are implicated in DNA control, the molecular mechanisms are unknown, in large part because the RNA.protein complexes are uncharacterized. Here, we identify a novel set of RNA-binding proteins that are well known for their function in chromatin regulation. The RNA-interacting proteins are components of the mammalian DNA methylation system. Genomic methylation controls chromatin in the context of transposon silencing, imprinting, and X chromosome dosage compensation. DNA methyltransferases (DNMTs) catalyze methylation of cytosines in CGs. The methyl-CGs are recognized by methyl-DNA-binding domain (MBD) proteins, which recruit histone deacetylases and chromatin remodeling proteins to effect silencing. We show that a subset of the DNMTs and MBD proteins can form RNA.protein complexes. We characterize the MBD protein RNA-binding activity and show that it is distinct from the methyl-CG-binding domain and mediates a high affinity interaction with RNA. The RNA and methyl-CG binding properties of the MBD proteins are mutually exclusive. We speculate that DNMTs and MBD proteins allow RNA molecules to participate in DNA methylation-mediated chromatin control.
引用
收藏
页码:49479 / 49487
页数:9
相关论文
共 71 条
  • [1] Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
    Amir, RE
    Van den Veyver, IB
    Wan, M
    Tran, CQ
    Francke, U
    Zoghbi, HY
    [J]. NATURE GENETICS, 1999, 23 (02) : 185 - 188
  • [2] Effects of Rett syndrome mutations of the methyl-CpG binding domain of the transcriptional repressor MeCP2 on selectivity for association with methylated DNA
    Ballestar, E
    Yusufzai, TM
    Wolffe, AP
    [J]. BIOCHEMISTRY, 2000, 39 (24) : 7100 - 7106
  • [3] LOSS OF METHYLATION ACTIVATES XIST IN SOMATIC BUT NOT IN EMBRYONIC-CELLS
    BEARD, C
    LI, E
    JAENISCH, R
    [J]. GENES & DEVELOPMENT, 1995, 9 (19) : 2325 - 2334
  • [4] MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1
    Bellacosa, A
    Cicchillitti, L
    Schepis, F
    Riccio, A
    Yeung, AT
    Matsumoto, Y
    Golemis, EA
    Genuardi, M
    Neri, G
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) : 3969 - 3974
  • [5] Role of MED1 (MBD4) gene in DNA repair and human cancer
    Bellacosa, A
    [J]. JOURNAL OF CELLULAR PHYSIOLOGY, 2001, 187 (02) : 137 - 144
  • [6] The DNA methyltransferases of mammals
    Bestor, TH
    [J]. HUMAN MOLECULAR GENETICS, 2000, 9 (16) : 2395 - 2402
  • [7] DNA methylation patterns and epigenetic memory
    Bird, A
    [J]. GENES & DEVELOPMENT, 2002, 16 (01) : 6 - 21
  • [8] 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
  • [9] CONSERVED STRUCTURES AND DIVERSITY OF FUNCTIONS OF RNA-BINDING PROTEINS
    BURD, CG
    DREYFUSS, G
    [J]. SCIENCE, 1994, 265 (5172) : 615 - 621
  • [10] Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    Cameron, EE
    Bachman, KE
    Myöhänen, S
    Herman, JG
    Baylin, SB
    [J]. NATURE GENETICS, 1999, 21 (01) : 103 - 107