Histone H4-K16 acetylation controls chromatin structure and protein interactions
Shogren-Knaak, Michael ; Ishii, Haruhiko ; Sun, Jian-Min ; Pazin, Michael J. ; Davie, James R. ; Peterson, Craig L.
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Keywords
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
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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.
Source
Science. 2006 Feb 10;311(5762):844-7. Link to article on publisher's site