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Science 10 February 2006:
Vol. 311. no. 5762, pp. 844 - 847
DOI: 10.1126/science.1124000

Reports

Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions

Michael Shogren-Knaak,1*{dagger} Haruhiko Ishii,1* Jian-Min Sun,2 Michael J. Pazin,3 James R. Davie,2 Craig L. Peterson1{ddagger}

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.

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.

{dagger} Present address: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, 4214 Molecular Biology Building, Ames, IA 50011, USA.

{ddagger} To whom correspondence should be addressed. E-mail: craig.peterson{at}umassmed.edu

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