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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.
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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

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DOI
10.1126/science.1124000
PubMed ID
16469925
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