Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
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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.
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The record
- Venue
- Science
- Topic
- Genomics and Chromatin Dynamics
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- University of Manitoba
- Funders
- National Institute of General Medical SciencesNational Institutes of Health
- Keywords
- Histone H4ChromatinChromatin remodelingAcetylationHistone H1Histone codeHistoneHistone H2ACell biologyHistone methyltransferaseHistone-modifying enzymesHistone octamerChemistryBiologyBiochemistryBiophysicsNucleosomeDNA
- Has abstract in OpenAlex
- yes