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Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Michael Shogren-Knaak,1*Haruhiko Ishii,1*Jian-Min Sun,2Michael J. Pazin,3James R. Davie,2Craig L. Peterson1
Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalentand 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 histoneH4 that was homogeneously acetylated at K16. The incorporationof this modified histone into nucleosomal arrays inhibits theformation of compact 30-nanometerlike fibers and impedesthe ability of chromatin to form cross-fiber interactions. H4-K16Acalso inhibits the ability of the adenosine triphosphateutilizingchromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome,indicating that this single histone modification modulates bothhigher order chromatin structure and functional interactionsbetween a nonhistone protein and the chromatin fiber.
1 Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. 2 Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Manitoba R3E0V9, Canada. 3 Laboratory of Cellular and Molecular Biology, National Institute on Aging, National Institutes of Health, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA.
* These authors contributed equally to this work.
Present address: Department of Biochemistry, Biophysics, andMolecular Biology, Iowa State University, 4214 Molecular BiologyBuilding, Ames, IA 50011, USA.
To whom correspondence should be addressed. E-mail: craig.peterson{at}umassmed.edu
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