Selective Association of the Trout-Specific H6 Protein with Chromatin Regions Susceptible to DNase I and DNase II: Possible Location of HMG-T in the Spacer Region between Core Nucleosomes

Nuclei and chromatin from trout testis cells were digested with three different nucleases (DNase I, DNase II, and micrococcal nuclease), and the acid-soluble proteins that were solubilized and those remaining bound to the nuclease-resistant DNA were compared electrophoretically. With the conditions...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1977-07, Vol.74 (7), p.2810-2814
Main Authors: Levy, Beatriz W., Norman C. W. Wong, Dixon, Gordon H.
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Biochemistry
Cell Nucleus - metabolism
Chromatin
Chromatin - ultrastructure
Chromosomal Proteins, Non-Histone - metabolism
Deoxyribonucleases - metabolism
DNA
DNA - metabolism
Electrophoresis
Gels
Genes
Histones
Male
Micrococcal Nuclease - metabolism
Nucleosomes
Protamines
Protein Binding
Starches
Testes
Testis
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Summary:Nuclei and chromatin from trout testis cells were digested with three different nucleases (DNase I, DNase II, and micrococcal nuclease), and the acid-soluble proteins that were solubilized and those remaining bound to the nuclease-resistant DNA were compared electrophoretically. With the conditions described by H. Weintraub and M. Groudine [(1976) Science, 193, 848-856], which we previously found to be selective in digesting actively transcribed regions in trout testis chromatin, a single chromosomal protein, H6, was solubilized. The nucleosomal histones and H1 remained insoluble, bound to the resistant DNA. In contrast, digestion with micrococcal nuclease led to a preferential solubilization of a second protein, HMG-T, together with the release of some nucleosomal histones and H1 into the soluble fraction. DNase II also discriminated between ``active'' and ``inactive'' chromatins; when a DNase II-solubilized ``active'' chromatin fraction was prepared, it too was enriched in H6 and HMG-T. Thus, both H6 and HMG-T, the two major low-salt extractable chromosomal nonhistone proteins from trout testis, are associated with chromatin regions selectively sensitive to nucleases. The preferential solubilization of HMG-T by micrococcal nuclease action suggests that it might be located at the internucleosomal ``spacer'' region.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.74.7.2810