Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions

• Published in: Science (American Association for the Advancement of Science) Vol. 311; no. 5762; pp. 844 - 847
• Main Authors: Shogren-Knaak, Michael, Ishii, Haruhiko, Sun, Jian-Min, Pazin, Michael J, Davie, James R, Peterson, Craig L
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 10-02-2006; The American Association for the Advancement of Science
• Subjects: Acetylation; Adenosine Triphosphate - metabolism; Biochemistry; Biological and medical sciences; Chromatin; Chromatin - chemistry; Chromatin - metabolism; Chromatin Assembly and Disassembly; Chromatin. Chromosome; Circles; DNA; DNA - metabolism; Drosophila Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Electrophoretic Mobility Shift Assay; Enzymes; Eukaryotes; Fundamental and applied biological sciences. Psychology; Gels; HeLa Cells; Histones; Histones - chemistry; Histones - metabolism; Humans; Ligation; Lysine - metabolism; Magnesium Chloride - pharmacology; Molecular and cellular biology; Molecular genetics; Nucleosomes; Nucleosomes - chemistry; Nucleosomes - metabolism; Protein Conformation; Protein Folding; Protein Processing, Post-Translational; Proteins; Recombinant Proteins - metabolism; Transcription Factors - metabolism; Posttranslational modification; Histone H4; Chromatin; Regulation(control); Enzyme; Use; Molecular interaction; Acetylation; Protein; Chromatin remodeling
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1124000

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.