DNA methylation and methyl-CpG binding proteins: developmental requirements and function

被引:324
作者
Bogdanovic, Ozren [1 ]
Veenstra, Gert Jan C. [1 ]
机构
[1] Radboud Univ Nijmegen, Dept Mol Biol, Fac Sci, Nijmegen Ctr Mol Life Sci, NL-6525 ED Nijmegen, Netherlands
关键词
DEPENDENT TRANSCRIPTIONAL REPRESSOR; CHROMATIN-REMODELING COMPLEX; EMBRYONIC STEM-CELLS; DE-NOVO METHYLATION; HISTONE DEACETYLASE COMPLEX; HONEYBEE APIS-MELLIFERA; RETT-SYNDROME; HUMAN CANCER; MAINTENANCE METHYLATION; MAMMALIAN DEVELOPMENT;
D O I
10.1007/s00412-009-0221-9
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
DNA methylation is a major epigenetic modification in the genomes of higher eukaryotes. In vertebrates, DNA methylation occurs predominantly on the CpG dinucleotide, and approximately 60% to 90% of these dinucleotides are modified. Distinct DNA methylation patterns, which can vary between different tissues and developmental stages, exist on specific loci. Sites of DNA methylation are occupied by various proteins, including methyl-CpG binding domain (MBD) proteins which recruit the enzymatic machinery to establish silent chromatin. Mutations in the MBD family member MeCP2 are the cause of Rett syndrome, a severe neurodevelopmental disorder, whereas other MBDs are known to bind sites of hypermethylation in human cancer cell lines. Here, we review the advances in our understanding of the function of DNA methylation, DNA methyltransferases, and methyl-CpG binding proteins in vertebrate embryonic development. MBDs function in transcriptional repression and long-range interactions in chromatin and also appear to play a role in genomic stability, neural signaling, and transcriptional activation. DNA methylation makes an essential and versatile epigenetic contribution to genome integrity and function.
引用
收藏
页码:549 / 565
页数:17
相关论文
共 212 条
  • [1] Isolation and initial characterization of a novel zinc finger gene, DNMT3L, on 21q22.3, related to the cytosine-5-methyltransferase 3 gene family
    Aapola, U
    Shibuya, K
    Scott, HS
    Ollila, J
    Vihinen, M
    Heino, M
    Shintani, A
    Kawasaki, K
    Minoshima, S
    Krohn, K
    Antonarakis, SE
    Shimizu, N
    Kudoh, J
    Peterson, P
    [J]. GENOMICS, 2000, 65 (03) : 293 - 298
  • [2] Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity
    Aapola, U
    Liiv, I
    Peterson, P
    [J]. NUCLEIC ACIDS RESEARCH, 2002, 30 (16) : 3602 - 3608
  • [3] Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2
    Adams, Valerie H.
    McBryant, Steven J.
    Wade, Paul A.
    Woodcock, Christopher L.
    Hansen, Jeffrey C.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (20) : 15057 - 15064
  • [4] MeCP2 interacts with HP1 and modulates its heterochromatin association during myogenic differentiation
    Agarwal, Noopur
    Hardt, Tanja
    Brero, Alessandro
    Nowak, Danny
    Rothbauer, Ulrich
    Becker, Annette
    Leonhardt, Heinrich
    Cardoso, M. Cristina
    [J]. NUCLEIC ACIDS RESEARCH, 2007, 35 (16) : 5402 - 5408
  • [5] 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
  • [6] Distinct role of long 3′ UTR BDNF mRNA in spine morphology and synaptic plasticity in hippocampal neurons
    An, Juan Ji
    Gharami, Kusumika
    Liao, Guey-Ying
    Woo, Newton H.
    Lau, Anthony G.
    Vanevski, Filip
    Torre, Enrique R.
    Jones, Kevin R.
    Feng, Yue
    Lu, Bai
    Xu, Baoji
    [J]. CELL, 2008, 134 (01) : 175 - 187
  • [7] TACC3 mediates the association of MBD2 with histone acetyltransferases and relieves transcriptional repression of methylated promoters
    Angrisano, T
    Lembo, F
    Pero, R
    Natale, F
    Fusco, A
    Avvedimento, VE
    Bruni, CB
    Chiariotti, L
    [J]. NUCLEIC ACIDS RESEARCH, 2006, 34 (01) : 364 - 372
  • [8] ANTEQUERA F, 1984, J BIOL CHEM, V259, P8033
  • [9] Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    Arita, Kyohei
    Ariyoshi, Mariko
    Tochio, Hidehito
    Nakamura, Yusuke
    Shirakawa, Masahiro
    [J]. NATURE, 2008, 455 (7214) : 818 - U12
  • [10] Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1
    Avvakumov, George V.
    Walker, John R.
    Xue, Sheng
    Li, Yanjun
    Duan, Shili
    Bronner, Christian
    Arrowsmith, Cheryl H.
    Dhe-Paganon, Sirano
    [J]. NATURE, 2008, 455 (7214) : 822 - U13