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Butyrate‐induced histone hyperacetylation in human and mouse cells: estimation of putative sites of histone acetylation in vivo
Author(s) -
Pantazis Panagiotis,
Bonner William M.
Publication year - 1982
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240200303
Subject(s) - acetylation , histone , in vivo , butyrate , chemistry , microbiology and biotechnology , biology , biochemistry , genetics , gene , fermentation
Human and mouse cells in culture were treated with various concentrations of sodium butyrate. Acid‐extracted histones of control and butyrate‐treated cells were analyzed by two‐dimensional gel electrophoresis. All core histones of the control cells contained modified forms. All core histones of the butyrate‐treated cells were hyperacetylated. Depending on the number of acetylation sites per molecule, each histone or histone variant exhibited a characteristic number of acetylated forms. This number was the same for each histone common in human and mouse cells treated with butyrate. Histones 2A.1, 2A.2, and 2A.X have two sites of inner acetylation; 2A.Z has 3; 2B's have 5; and each one of the H3 variants as well as H4 have 4.