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Arginine methylation of the histone h3 tail impedes effector binding.

Arginine methylation of the histone h3 tail impedes effector binding. Research Abstract Details 

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  • Arginine methylation of the histone h3 tail impedes effector binding. Abstract Text:

    aimee n ibergAimee N Iberg,alexsandra espejoAlexsandra Espejo,donghang chengDonghang Cheng,daehoon kimDaehoon Kim,jonathan michaud-levesqueJonathan Michaud-Levesque,stephane richardStephane Richard,mark t bedfordMark T Bedford,aimee n ibergAimee N Iberg,alexsandra espejoAlexsandra Espejo,donghang chengDonghang Cheng,daehoon kimDaehoon Kim,jonathan michaud-levesqueJonathan Michaud-Levesque,stephane richardStephane Richard,mark t bedfordMark T Bedford,

    Histone tail post-translational modification results in changes in cellular processes, either by generating or blocking docking sites for histone code readers or by altering the higher order chromatin structure. H3K4me3 is known to mark the promoter regions of active transcription. Proteins bind H3K4 in a methyl-dependent manner and aid in the recruitment of histone-remodeling enzymes and transcriptional cofactors. The H3K4me3 binders harbor methyl-specific chromatin binding domains, including plant homeodomain, Chromo, and tudor domains. Structural analysis of the plant homeodomains present in effector proteins, as well as the WD40 repeats of WDR5, reveals critical contacts between residues in these domains and H3R2. The intimate contact between H3R2 and these domain types leads to the hypothesis that methylation of this arginine residue antagonizes the binding of effector proteins to the N-terminal tail of H3. Here we show that H3 tail binding effector proteins are indeed sensitive to H3R2 methylation and that PRMT6, not CARM1/PRMT4, is the primary methyltransferase acting on this site. We have tested the expression of a select group of H3K4 effector-regulated genes in PRMT6 knockdown cells and found that their levels are altered. Thus, PRMT6 methylates H3R2 and is a negative regulator of N-terminal H3 tail binding.

    Arginine methylation of the histone h3 tail impedes effector binding. Publishing Authors By Initials

    an ibergAN Iberg,a espejoA Espejo,d chengD Cheng,d kimD Kim,j michaud-levesqueJ Michaud-Levesque,s richardS Richard,mt bedfordMT Bedford,an ibergAN Iberg,a espejoA Espejo,d chengD Cheng,d kimD Kim,j michaud-levesqueJ Michaud-Levesque,s richardS Richard,mt bedfordMT Bedford,

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    Arginine methylation of the histone h3 tail impedes effector binding. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: The Journal of biological chemistry

    VOLUME: 283

    Page Numbers: 3006-10

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 11

    MONTH: 12

    YEAR: 2007

    Arginine methylation of the histone h3 tail impedes effector binding. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985121

    Arginine methylation of the histone h3 tail impedes effector binding. Keywords Mesh Terms:

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    Grant and Affiliation Information for Arginine methylation of the histone h3 tail impedes effector binding.

    AFFILIATION: The University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, Smithville, Texas 78957.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Biol Chem

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