TY - JOUR
T1 - Nucleosomal structure as probed by H3 histone thiol reactivity - Conformation of H3 histone variants is differently affected by thiol group reagents
AU - Ferrari, Nicoletta
AU - Pfeffer, Ulrich
AU - Vidali, Giorgio
PY - 1987/2
Y1 - 1987/2
N2 - 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 to N-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.
AB - 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 to N-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.
KW - H3 thiol reactivity
KW - histone acetylation
KW - Nucleosonal structure
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U2 - 10.1007/BF02797069
DO - 10.1007/BF02797069
M3 - Article
C2 - 2440574
AN - SCOPUS:0023285974
VL - 10
SP - 1
EP - 13
JO - Cell Biochemistry and Biophysics
JF - Cell Biochemistry and Biophysics
SN - 1085-9195
IS - 1
ER -