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Nucleosomal structure as probed by H3 histone thiol reactivity. Conformation of H3 histone variants is differently affected by thiol group reagents.

Authors :
Ferrari N
Pfeffer U
Vidali G
Source :
Cell biophysics [Cell Biophys] 1987 Feb; Vol. 10 (1), pp. 1-13.
Publication Year :
1987

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 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.

Details

Language :
English
ISSN :
0163-4992
Volume :
10
Issue :
1
Database :
MEDLINE
Journal :
Cell biophysics
Publication Type :
Academic Journal
Accession number :
2440574
Full Text :
https://doi.org/10.1007/BF02797069