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. 2006 Feb 10;311(5762):844-7.
doi: 10.1126/science.1124000.

Histone H4-K16 acetylation controls chromatin structure and protein interactions

Michael Shogren-Knaak  1 , Haruhiko Ishii, Jian-Min Sun, Michael J Pazin, James R Davie, Craig L Peterson
Affiliations

Histone H4-K16 acetylation controls chromatin structure and protein interactions

Michael Shogren-Knaak et al. Science. .

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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