Histone H4-K16 acetylation controls chromatin structure and protein interactions |
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Authors: | Shogren-Knaak Michael Ishii Haruhiko Sun Jian-Min Pazin Michael J Davie James R Peterson Craig L |
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Institution: | Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. |
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Abstract: | Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber. |
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