Methyl-CpG-binding proteins: Targeting specific gene repression

European Journal of Biochemistry

Volumn 268, Issue 1, 2001, Pages 1-6

  Ballestar, Esteban ^a   Wolffe, Alan P ^b  

^a UNIVERSITY OF VALENCIA   (Spain)

^b SANGAMO BIOSCIENCES INC   (United States)

Author keywords

DNA methylation; Gene repression; Histone deacetylase; MeCP2; Methyl CpG binding domain (MBD)

Indexed keywords

ENDONUCLEASE; HISTONE DEACETYLASE; METHYL CPG BINDING PROTEIN; METHYL GROUP; MONOMER; UNCLASSIFIED DRUG;

ANIMAL CELL; BASE MISPAIRING; CONTROLLED STUDY; CPG ISLAND; DNA METHYLATION; DNA MODIFICATION; DNA SEQUENCE; GENE REPRESSION; GENE TARGETING; GENOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; ANIMALS; CHROMOSOMAL PROTEINS, NON-HISTONE; CPG ISLANDS; DNA; DNA METHYLATION; DNA-BINDING PROTEINS; GENE SILENCING; HUMANS; METHYL-CPG-BINDING PROTEIN 2; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; TRANSCRIPTION, GENETIC;

ANIMALIA; EUKARYOTA; VERTEBRATA;

EID: 0035169663     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.01869.x     Document Type: Review

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4. DNA methylation inhibits transcription indirectly via a methyl-CpG binding protein
5. Organization of 5-methylcytosine in chromosomal DNA
6. Specific protection of methylated CpGs in mammalian nuclei
7. Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs
8. Component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins
9. MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex
10. Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2
11. MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin
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13. De novo DNA cytosine methyltransferase activities in mouse embryonic stem cells
14. A mammalian protein with specific demethylase activity for mCpG
15. Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation
16. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
17. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
18. Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1
19. Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein
20. Effects of rett syndrome mutations of the methyl-CpG binding domain of the transcriptional repressor MeCP2 on selectivity for association with methylated DNA
21. The solution structure of the domain from MeCP2 that binds to methylated DNA
22. Characterisation of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA
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24. Nucleosomes inhibit the iniciation of transcription but allow chain elongation with the displacement of histones
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32. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
33. Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription
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35. Mechanism of transcriptional regulation by methyl-CpG binding protein MBD1
36. A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
37. MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase