Abstract
Complexes of histone H1 from calf thymus with high molecular weight DNA have been studied. Stuctural changes within a molecule of histone H1 and its binding with DNA were registered over the fluorescence of a single residue of tyrosine in H1 whereas the changes in compaction of DNA were registered turbidimetrically. Association constants of the histone H1 globular domain with DNA were found on the basis of fluorescence measurements at different concentrations of salt and urea. It is shown that, at physiological ionic strength, compaction of DNA, folding of the histone H1 globular domain and sharp weakening of the latter's binding with DNA take place. The DNA compaction does not depend on the presence of urea in solution. It is concluded that the histone H1 globular domain is not involved in DNA compaction in chromatin. The role of various structural regions of histone H1 in chromatin structure stabilization is discussed.
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