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Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin.

Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Research Abstract Details 

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  • Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Abstract Text:

    tatiana nikitinaTatiana Nikitina,xi shiXi Shi,rajarshi p ghoshRajarshi P Ghosh,rachel a horowitz-schererRachel A Horowitz-Scherer,jeffrey c hansenJeffrey C Hansen,christopher l woodcockChristopher L Woodcock,

    Mutations of the methylated DNA binding protein MeCP2, a multifunctional protein that is thought to transmit epigenetic information encoded as methylated CpG dinucleotides to the transcriptional machinery, give rise to the debilitating neurodevelopmental disease Rett syndrome (RTT). In this in vitro study, the methylation-dependent and -independent interactions of wild-type and mutant human MeCP2 with defined DNA and chromatin substrates were investigated. A combination of electrophoretic mobility shift assays and visualization by electron microscopy made it possible to understand the different conformational changes underlying the gel shifts. MeCP2 is shown to have, in addition to its well-established methylated DNA binding domain, a methylation-independent DNA binding site (or sites) in the first 294 residues, while the C-terminal portion of MeCP2 (residues 295 to 486) contains one or more essential chromatin interaction regions. All of the RTT-inducing mutants tested were quantitatively bound to chromatin under our conditions, but those that tend to be associated with the more severe RTT symptoms failed to induce the extensive compaction observed with wild-type MeCP2. Two modes of MeCP2-driven compaction were observed, one promoting nucleosome clustering and the other forming DNA-MeCP2-DNA complexes. MeCP2 binding to DNA and chromatin involves a number of different molecular interactions, some of which result in compaction and oligomerization. The multifunctional roles of MeCP2 may be reflected in these different interactions.

    Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Publishing Authors By Initials

    t nikitinaT Nikitina,x shiX Shi,rp ghoshRP Ghosh,ra horowitz-schererRA Horowitz-Scherer,jc hansenJC Hansen,cl woodcockCL Woodcock,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation research

    PUBMED ID PMID:

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    Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Molecular and cellular biology

    VOLUME: 27

    Page Numbers: 864-77

    Journal Abbreviation: Mol. Cell. Biol.

    ISSN: 0270-7306

    DAY: 13

    MONTH: 11

    YEAR: 2006

    Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8109087

    Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Keywords Mesh Terms:

    KEYWORDS: Protein Conformation

    MESH TERMS: ultrastructure

    Chemical & Substance for Abstract: Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin. Information

    Substance Name: DNA

    Registry Number: 9007-49-2

    Grant and Affiliation Information for Multiple modes of interaction between the methylated DNA binding protein MeCP2 and chromatin.

    AFFILIATION: Biology Department, University of Massachusetts, Amherst, MA 01003, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM 66834

    ACRONYM: GM

    MEDLINETA: Mol Cell Biol

    REFSOURCE:

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    ACCESSION NUMBER:

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