Histone H4-K16 acetylation controls chromatin structure and protein interactions
Program in Molecular Medicine
Acetylation; Adenosine Triphosphate; Chromatin; *Chromatin Assembly and Disassembly; DNA; Drosophila Proteins; Electrophoresis, Polyacrylamide Gel; Electrophoretic Mobility Shift Assay; Hela Cells; Histones; Humans; Lysine; Magnesium Chloride; Nucleosomes; Protein Conformation; Protein Folding; Protein Processing, Post-Translational; Recombinant Proteins; Transcription Factors
Life Sciences | Medicine and Health Sciences
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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Citation: Science. 2006 Feb 10;311(5762):844-7. Link to article on publisher's site
DOI of Published Version
Science (New York, N.Y.)
Shogren-Knaak, Michael; Ishii, Haruhiko; Sun, Jian-Min; Pazin, Michael J.; Davie, James R.; and Peterson, Craig L., "Histone H4-K16 acetylation controls chromatin structure and protein interactions" (2006). Open Access Articles. 1632.