学術雑誌論文 Covalent modifications of histone H3K9 promote binding of CHD3

A. H., Tencer,  ,  K.L., Cox,  ,  D., Luo,  ,  J. B., Bridgers,  ,  J, Lyu,  ,  X., Wang,  ,  J. K., Sims,  ,  T.M., Weaver,  ,  H. F., Allen,  ,  Y., Zhang,  ,  J., Gatchalian,  ,  M., Darcy,  ,  M., Gibson,  ,  J., Ikebe,  ,  W., Li,  ,  P.A., Wade,  ,  J.J., Hayes,  ,  B. D., Strahl,  ,  H., Kono,  ,  M .G., Poirier,  ,  C. A., Musselman,  ,  T. G., Kutateladze,

21 ( 2 )  , pp.455 - 465 , 2017-10
ISSN:2211-1247
内容記述
Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) whose functional significance is not well established. Here, we show that CHD3 co-localizes with the other NuRD subunits, including HDAC1, near the H3K9ac-enriched promoters of the NuRD target genes. The tandem PHD fingers of CHD3 bind histone H3 tails and posttranslational modifications that increase hydrophobicity of H3K9-methylation or acetylation (H3K9me3 or H3K9ac)-enhance this interaction. Binding of CHD3 PHDs promotes H3K9Cme3-nucleosome unwrapping in vitro and perturbs the pericentric heterochromatin structure in vivo. Methylation or acetylation of H3K9 uniquely alleviates the intra-nucleosomal interaction of histone H3 tails, increasing H3K9 accessibility. Collectively, our data suggest that the targeting of covalently modified H3K9 by CHD3 might be essential in diverse functions of NuRD.

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