We have investigated using the DNA binding fluorochromes 7-aminoactinomycin (7-AAMD) and 48,6diamidino-2-phenylindole (DAPI) as cytochemical probes for linker histone (H1)-chromatin interactions in situ. Human lymphocytes, permeabilized with digitonin, were exposed to increasing concentrations of so
On the binding of histone H1 in chromatin
β Scribed by Robert C. Krueger
- Publisher
- Springer
- Year
- 1986
- Tongue
- English
- Weight
- 448 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0301-4851
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β¦ Synopsis
Nucleosomal subunits isolated from rabbit thymus nuclei in 0.04 M K2SO 4-0.02 M Tris, pH 7.4 were devoid of histone H1, while whole chromatin prepared in the same buffer contained the full complement of histone HI. The question is asked why histone H1 dissociates from the subunits but not from the high molecular weight material. We propose that, at physiological salt concentrations, histone H1 is not bound to linker DNA as depicted in the current models; rather, alternate attachment sites, present only in the polymer, are involved.
π SIMILAR VOLUMES
The aim of this work was to study the accessibility of histone H1(0) and its structural domains to antibody binding in high molecular mass chromatin fragments of different conformations. Three types of specific antibody populations were used: (1) anti-H1(0) which reacted with antigenic determinants