Biopolym. Cell. 1986; 2(1):39-44, 55.
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


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.


[1] Thoma F, Koller T, Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol. 1979;83(2 Pt 1):403-27.
[2] Thoma F, Koller T. Unravelled nucleosomes, nucleosome beads and higher order structures of chromatin: influence of non-histone components and histone H1. J Mol Biol. 1981;149(4):709-33.
[3] Varshavsky AJ, Bakayev VV, Georgiev GP. Heterogeneity of chromatin subunits in vitro and location of histone H1. Nucleic Acids Res. 1976;3(2):477-92.
[4] Cowman MK, Fasman GD. Dependence of mononucleosome deoxyribonucleic acid conformation on the deoxyribonucleic acid length and H1/H5 content. Circular dichroism and thermal denaturation studies. Biochemistry. 1980;19(3):532-41.
[5] Belyavsky AV, Bavykin SG, Goguadze EG, Mirzabekov AD. Primary organization of nucleosomes containing all five histones and DNA 175 and 165 base-pairs long. J Mol Biol. 1980;139(3):519-36.
[6] Ring D, Cole RD. Chemical cross-linking of H1 histone to the nucleosomal histones. J Biol Chem. 1979;254(22):11688-95.
[7] Fasman GD, Schaffhausen B, Goldsmith L, Adler A. Conformational changes associated with f-1 histone-deoxyribonucleic acid complexes. Circular dichroism studies. Biochemistry. 1970;9(14):2814-22.
[8] Hsiang MW, Cole RD. Structure of histone H1-DNA complex: effect of histone H1 on DNA condensation. Proc Natl Acad Sci U S A. 1977;74(11):4852-6.
[9] Bradbury EM, Danby SE, Rattle HW, Giancotti V. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. Histone H1 in chromatin and in H1 - DNA complexes. Eur J Biochem. 1975;57(1):97-105.
[10] Hartman PG, Chapman GE, Moss T, Bradbury EM. Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule. Eur J Biochem. 1977;77(1):45-51.
[11] Smerdon MJ, Isenberg I. Conformational changes in subfractions of calf thymus histone H1. Biochemistry. 1976;15(19):4233-42.
[12] Chapman GE, Hartman PG, Cary PD, Bradbury EM, Lee DR. A nuclear-magnetic-resonance study of the globular structure of the H1 histone. Eur J Biochem. 1978;86(1):35-44.
[13] Bradbury EM, Chapman GE, Danby SE, Hartman PG, Riches PL. Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. The properties of the N-terminal and C-terminal halves of histone H1. Eur J Biochem. 1975;57(2):521-8.
[14] Khrapunov SN, Dragan AI, Sivolob AV, Kadura SN, Berdyshev GD. Peculiarities of the amino acid composition, spatial organization and interaction with DNA of histones H1 from calf thymus and carp spermatozoa. Biokhimiia. 1983;48(7):1085-94.
[15] Johns EW. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964;92(1):55-9.
[16] Felsenfeld G, Hirschman SZ. A neighbor-interaction analysis of the hypochromism and spectra of DNA. J Mol Biol. 1965;13(2):407-27.
[17] Khrapunov SN, Dragan AI, Protas AF, Berdyshev GD. Spatial organization of the histone dimer H2A-H2B in solutions of different ionic strengths. Mol Biol (Mosk). 1983;17(5):992-1000.
[18] Kelly RC, Jensen DE, von Hippel PH. DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides. J Biol Chem. 1976;251(22):7240-50.
[19] Khrapunov SN, Protas AF, Sivolob AV, Dragan AI, Berdyshev GD. Characteristics of the tertiary structure of histone H1 from the calf thymus. Mol Biol (Mosk). 1984;18(4):979-87.
[20] Record MT Jr, Anderson CF, Lohman TM. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Q Rev Biophys. 1978;11(2):103-78.
[21] Manning GS. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q Rev Biophys. 1978;11(2):179-246.
[22] Manning GS. Theory of H1-mediated control of higher orders of structure in chromatin. Biopolymers. 1979;18(12):2929-42.
[23] Manning GS. Thermodynamic stability theory for DNA doughnut shapes induced by charge neutralization. Biopolymers. 1980;19(1):37-59.
[24] Bloomfield VA, Wilson RW, Rau DC. Polyelectrolyte effects in DNA condensation by polyamines. Biophys Chem. 1980;11(3-4):339-43.
[25] Glotov BO, Nikolaev LG, Severin ES. Histone H1--DNA interaction. On the mechanism of DNA strands crosslinking by histone H1. Nucleic Acids Res. 1978;5(7):2587-605.
[26] Allan J, Hartman PG, Crane-Robinson C, Aviles FX. The structure of histone H1 and its location in chromatin. Nature. 1980;288(5792):675-9.
[27] Singer DS, Singer MF. Studies on the interaction of H1 histone with superhelical DNA: characterization of the recognition and binding regions of H1 histones. Nucleic Acids Res. 1976;3(10):2531-47.
[28] Undritsov IM, Naktinis VI, Vengerov IuIu, Vashakidze RP, Karpenchuk KG. Complexes of histone H1 with supercoiled DNA. Mol Biol (Mosk). 1982;16(4):720-30.