Nucleosomal structure as probed by H3 histone thiol reactivity |
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Authors: | Nicoletta Ferrari Ulrich Pfeffer Giorgio Vidali |
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Affiliation: | (1) Molecular Biology Laboratory, Istituto Nazionale per la Ricerca sul Cancro, Viale Benedetto XV 10, 16132 Genova, Italy;(2) Institut fuer Biochemie und Molekularbiologie, Freie Universitaet Berlin, Ehrenbergstr, 26-28, 1 Berlin 33, FRG |
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Abstract: | Two H3 histone variants are found in equal amount in HeLa cells, and they have been characterized by two-dimensional gel electrophoresis followed by reaction with specific antibodies. These molecules are the only cysteine-containing histones, and they have been used as the target for thiol-specific reagents, in intact nuclei, isolated nucleosomes, histone complexes, and purified histones. Cysteine residues are available toN-ethylmaleimide only when histones are disassembled from the core particles. Upon reaction with these reagents, one of the H3 variants undergoes profound conformational changes, as revealed by an altered electrophoretic mobility. |
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Keywords: | Nucleosonal structure H3 thiol reactivity histone acetylation |
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