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Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver
- Source :
- FEBS Letters; January 1998, Vol. 421 Issue: 2 p109-114, 6p
- Publication Year :
- 1998
-
Abstract
- The cytoplasmic B-type histone acetyltransferase was purified to apparent homogeneity from maize embryos. We established a novel protocol for easy large-scale preparation of acetylated core histone species, using preparative acetic acid-urea-Triton PAGE. The pure maize histone acetyltransferase B was highly specific for histone H4 under various assay conditions, modifying H4 up to the di-acetylated isoform. Only non-acetylated H4 isoform was accepted as substrate, whereas mono-acetylated H4 could not be further acetylated. The enzyme selectively acetylated lysines 12 and 5 in a sequential manner. The same results were obtained with a partially purified cytoplasmic histone acetyltransferase of rat liver. Protein sequencing results were supported by immunological characterization of acetylated H4 subspecies with site-specific H4-acetyllysine antibodies.
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 421
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- FEBS Letters
- Publication Type :
- Periodical
- Accession number :
- ejs2504013
- Full Text :
- https://doi.org/10.1016/S0014-5793(97)01544-5