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Cell Rep
2017 Oct 10;212:455-466. doi: 10.1016/j.celrep.2017.09.054.
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Covalent Modifications of Histone H3K9 Promote Binding of CHD3.
Tencer AH
,
Cox KL
,
Di L
,
Bridgers JB
,
Lyu J
,
Wang X
,
Sims JK
,
Weaver TM
,
Allen HF
,
Zhang Y
,
Gatchalian J
,
Darcy MA
,
Gibson MD
,
Ikebe J
,
Li W
,
Wade PA
,
Hayes JJ
,
Strahl BD
,
Kono H
,
Poirier MG
,
Musselman CA
,
Kutateladze TG
.
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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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