Histone H1--DNA interaction. On the mechanism of DNA strands crosslinking by histone H1.

TitleHistone H1--DNA interaction. On the mechanism of DNA strands crosslinking by histone H1.
Publication TypeJournal Article
Year of Publication1978
AuthorsGlotov BO, Nikolaev LG, Severin ES
JournalNucleic Acids Res
Volume5
Issue7
Pagination2587-605
Date Published1978 Jul
ISSN0305-1048
KeywordsCations, Divalent, Chromatin, DNA, Histones, Hydrogen Bonding, Hydrogen-Ion Concentration, Nephelometry and Turbidimetry, Osmolar Concentration, Peptide Fragments, Phosphates, Protein Binding, Sodium Chloride, Structure-Activity Relationship
Abstract

Crosslinking of DNA fibers by histone H1 or phosphorylated on Ser-37 histone H1, and by the individual fragments of the H1 polypeptide chain was studied by the method of turbidimetry. The dependence of the turbidity of DNA-protein complexes on the ionic strength in solution suggests that the condensation of H1.DNA complexes in vitro is apparently due to both specific histone-DNA interactions with the contribution of hydrogen and/or hydrophobic bonds and the formation of polycationic "bridges" fastening the DNA fibers. The effectiveness of the condensation is postulated to be a function of a proportion between the two mechanisms which in turn can be controlled by slight changes in ionic surroundings. The sharp dependence of shrinkage of H1.DNA complexes on ionic strength at "physiological" salt concentrations could provide a mechanism to regulate density and consequently the total activity of chromatin in the cell nuclei. The phosphorylation of histone H1 on Ser-37 by a specific histone kinase does not noticeably affect the pattern of DNA crosslinking by the H1.

DOI10.1093/nar/5.7.2587
Alternate JournalNucleic Acids Res
PubMed ID27766
PubMed Central IDPMC342188

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