Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
University of Massachusetts Chan Medical School · Institute on Aging · +3 more institutions
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…
Citation impact
- FWCI
- 44.84
- Percentile
- 100%
- References
- 25
Authors
6- MAMichael A. Shogren‐KnaakCorresponding
University of Massachusetts Chan Medical School, Institute on Aging, National Institute on Aging, University of Manitoba
- HIHaruhiko IshiiCorresponding
University of Massachusetts Chan Medical School, Institute on Aging, National Institute on Aging, University of Manitoba
- JSJian-Min Sun
University of Massachusetts Chan Medical School, Institute on Aging, National Institute on Aging, University of Manitoba
- MJMichael J. Pazin
National Institutes of Health, University of Massachusetts Chan Medical School, Institute on Aging, National Institute on Aging, University of Manitoba
- JDJames Davie
University of Massachusetts Chan Medical School, Institute on Aging, National Institute on Aging, University of Manitoba
Topics & keywords
- Histone H4
- Chromatin
- Chromatin remodeling
- Acetylation
- Histone H1
- Histone code
- Histone
- Histone H2A