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Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver
Author(s) -
Kölle Doris,
Sarg Bettina,
Lindner Herbert,
Loidl Peter
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01544-5
Subject(s) - histone acetyltransferases , acetyltransferases , cytoplasm , substrate specificity , substrate (aquarium) , biochemistry , acetylation , histone , chemistry , genetics , biology , enzyme , gene , ecology
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.