Enzymic Acetylation of Nucleosome Histone1
- 1 November 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 84 (5), 1203-1207
- https://doi.org/10.1093/oxfordjournals.jbchem.a132237
Abstract
Rat liver chromatin prepared from purified nuclei catalyzed the acetylation of histones in nucleosomes at the same level as that of nuclei. The activity of histone acetyltransferase in chromatin was destroyed by heat treatment at 65°C for 5 min. Histones in exogenously added nucleosomes also served as substrate for the enzyme. The sites of acetylation in the nucleosomes appeared to be in the trypsin-digestable N-terminal regions of histones H4, H3, and H2A, as has been reported in an in vivo system.This publication has 5 references indexed in Scilit:
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- Chromatin subunits contain normal levels of major acetylated histone species.Journal of Biological Chemistry, 1977
- Physical properties of chemically acetylated rat liver chromatin.Proceedings of the National Academy of Sciences, 1977
- Action of micrococcal nuclease on chromatin and the location of histone H1Journal of Molecular Biology, 1977
- Activation of chromatin by acetylation of histone side chains.Proceedings of the National Academy of Sciences, 1976