Abstract
We have investigated the interactions of the methyl-CpG binding transcriptional repressor MeCP2 with nucleosomal DNA. We find that MeCP2 forms discrete complexes with nucleosomal DNA associating with methyl-CpGs exposed in the major groove via the methyl-CpG-binding domain (MBD). In addition to the MBD, the carboxyl-terminal segment of MeCP2 facilitates binding both to naked DNA and to the nucleosome core. These observations provide a molecular mechanism by which MeCP2 can gain access to chromatin in order to target corepressor complexes that further modify chromatin structure.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chromosomal Proteins, Non-Histone*
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CpG Islands / genetics*
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DNA / metabolism
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DNA Footprinting
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DNA Methylation*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / isolation & purification
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DNA-Binding Proteins / metabolism*
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Deoxyribonuclease I
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Fabaceae
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Glutathione Transferase / genetics
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Hydrolysis
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Methyl-CpG-Binding Protein 2
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Micrococcal Nuclease / metabolism
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Nucleosomes / genetics
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Nucleosomes / metabolism
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Plant Proteins / metabolism
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Plants, Medicinal
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Protein Binding
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RNA, Ribosomal, 5S / genetics
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RNA, Ribosomal, 5S / metabolism
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Repressor Proteins / genetics
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Repressor Proteins / isolation & purification
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Repressor Proteins / metabolism*
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Sequence Deletion
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Xenopus
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Xenopus laevis
Substances
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Chromosomal Proteins, Non-Histone
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DNA-Binding Proteins
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Methyl-CpG-Binding Protein 2
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Nucleosomes
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Plant Proteins
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RNA, Ribosomal, 5S
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Recombinant Fusion Proteins
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Recombinant Proteins
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Repressor Proteins
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phaseolin protein, Phaseolus vulgaris
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DNA
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Glutathione Transferase
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Deoxyribonuclease I
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Micrococcal Nuclease