Biopolym. Cell. 1986; 2(1):39-44, 55.
http://dx.doi.org/10.7124/bc.000199
Genome and Its Regulation
The peculiarities of the H1 histone-DNA interaction
1Khrapunov S. N., 1Sivolob A. V., 1Kucherenko N. E.
  1. Taras Shevchenko State University of Kiev
    Kiev, USSR

Abstract

The complexes of HI histone from the calf thymus with DNA are studied. Structural changes within a molecule of H1 histone and its binding with DNA are registered by the fluorescence of the single tyrosine residue in H1 whereas the changes in compactination of DNA are registered turbidimetrically. Association constants of the H1 histone globular part with DNA were found on the basis of fluorescence measurements at the different concentration of salt and urea. It is shown that physiological ionic strength induces compactization of DNA, folding of the globular part of H1 histone and a sharp decrease of its binding with DNA. The DNA compactization does not depend on the urea presence in the solution. It is possible to conclude that the globular part of HI histone is not involved in DNA compactization in chromatin. The role of various structural regions of histone H1 in chromatin structure stabilization is discussed.
Full text: (PDF, in Russian)

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