Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver

FEBS Letters

Sarg, Bettina²  Lindner, Herbert²  Loidl, Peter¹  Kölle, Doris¹ 

[1] Department of Microbiology, University of Innsbruck Medical School, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria;Department of Medical Chemistry and Biochemistry, University of Innsbruck Medical School, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria

关键词: Chromatin;    Histone acetylation;    Histone acetyltransferase;    Nucleosome assembly;    Maize;    Histone H4;   

DOI  :  10.1016/S0014-5793(97)01544-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown