Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver.
FEBS Lett
; 421(2): 109-14, 1998 Jan 09.
Article
em En
| MEDLINE
| ID: mdl-9468289
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Acetiltransferases
/
Zea mays
/
Proteínas de Saccharomyces cerevisiae
/
Fígado
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Áustria