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      Histone H4-K16 acetylation controls chromatin structure and protein interactions.

      Science (New York, N.Y.)

      metabolism, Acetylation, Transcription Factors, Recombinant Proteins, Protein Processing, Post-Translational, Protein Folding, Protein Conformation, chemistry, Nucleosomes, pharmacology, Magnesium Chloride, Lysine, Humans, Histones, HeLa Cells, Electrophoretic Mobility Shift Assay, Electrophoresis, Polyacrylamide Gel, Drosophila Proteins, DNA, Chromatin Assembly and Disassembly, Chromatin, Adenosine Triphosphate

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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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          Journal
          10.1126/science.1124000
          16469925

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