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Histone H4 acetylation in Drosophila Frequency of acetylation at different sites defined by immunolabelling with site‐specific antibodies
Author(s) -
Munks Rebecca J.L.,
Moore Jayne,
O'Neill Laura P.,
Turner Bryan M.
Publication year - 1991
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 - 10.1016/0014-5793(91)80695-y
Subject(s) - acetylation , histone , histone h4 , antibody , microbiology and biotechnology , chemistry , biology , biochemistry , genetics , gene
Electrophoresis, Western blotting and immunostaining with antibodies specific for histone H4 acetylated at lysines 5, 8, 12, or 16, were used to define patterns of H4 acetylation in cell lines from humans (HL60) and the fruit fly Drosophila (S2, Kc). In human cells, the mono‐acetylated isoform H4Ac 1 is acetylated predominantly at just one of the four possible lysine residues, lysine 16. This is the first step in the progressive acetylation of H4. In contrast, in Drosophila , H4Ac 1 is acetylated at lysines 5, 8, or 12 with approximately equal frequency. Fundamental differences appear to exist in control of H4 acetylation in different species, despite the evolutionary conservation of acetylation sites.