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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.·2006·Science

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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Metadata

Authors
Shogren-Knaak, M., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J. R., & Peterson, C. L.
Venue
Science
Published
2006-02-10
Volume
311
Issue
5762
Pages
844-847
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2069328568
Cited by
1,873
References
0
FWCI
40.40
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions. https://app.cochat.ai/papers/10.1126/science.1124000
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Shogren-Knaak, M., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J. R., & Peterson, C. L. (2006). Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions. Science. https://doi.org/10.1126/science.1124000

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