Biopolym. Cell. 1985; 1(4):179-182.
Structure and Function of Biopolymers
The role of polyanions as DNA conformons and competitors in chromatin organization
1Paponov V. D.
  1. Institute of Medical Genetics, Academy of Medical Sciences of the USSR
    Moscow, USSR


Polyanionic components of cell nucleus participating in chromatin organization may be devided into two classes. The first class of permanent and transitive conformons provides specific conformations of DNA fragments and/or special states of corresponding sites of chromatin fibers for a long and short period of time, respectively. The second class of polyanions fulfils the role of competitors with DNA for the chromatin components. So-called В«factors of chromatin assembly occurring in some cells as complexes with molecules of nonchromosomal histone pool are representatives of the second class of the nuclear polyanions. The functional role of formation of the above complexes may be in prevention of histone competition for DNA, which causes in vitro the assembly or reorganization of chromatin into the nucleoprotein completely devoid of the histone HI even at 1.5–2-fold weight excess of the whole histone over DNA.


[1] Kanungu M. Biochemistry of aging. M. : Mir, 1982. 294 p.
[2] Chemical Encyclopedic Dictionary, ed. ILKnunyants. Sov. entsikl., 1983. 792 p.
[3] Wells RD, Goodman TC, Hillen W, Horn GT, Klein RD, Larson JE, M?ller UR, Neuendorf SK, Panayotatos N, Stirdivant SM. Prog Nucleic Acid Res Mol Biol. 1980;24:167-267.
[4] Johns EW, Butler JA. Specificity of the interactions between histones and deoxyribonucleic acid. Nature. 1964;204:853-5.
[5] Paponov VD. Competitive binding of histones to DNA and the problem of chromatin self-assembly. Biokhimiia. 1980;45(9):1539-48.
[6] Ashmarin IP, Muratchaeva PS. Competitive relationships among histone fractions during interaction with DNA. Biokhimiia. 1969;34(6):1250-6.
[7] Samal B. Transcription of eukaryotic genome. N. Y. : Acad. Press, 1980 370 p.
[8] Voordouw G, Kalif D, Eisenberg H. Studies of ColE1-plasmid DNA and its interactions with histones: sedimentation velocity studies of monodisperse complexes reconstituted with calf-thymus histones. Nucleic Acids Res. 1977;4(5):1207-23.
[9] Vashakidze RP, Karpenchuk KG, Naktinis VI, Undritsov IM, Mirzabekov AD. Drosophila melanogaster embryo factor capable of supercoiling circular covalently closed DNA in the presence of core histones H2a, H2b, H3, H4 or protamine. Biokhimiia. 1980;45(4):718-22.
[10] Paponov VD, Gromov PS, Bogdanov VV, Spitkovskii DM. Histone competition for DNA and its possible role in the self-assembly of eu- and heterochromatin. Biull Eksp Biol Med. 1981;91(5):548-50.
[11] Paponov VD, Gromov PS, Spitkovskii DM. Selective loss of histone H1 as a new chromatin reaction to the addition of total histone in a medium of physiological ionic strength. Biull Eksp Biol Med. 1982;94(11):31-3.
[12] Grellet F, Delseny M, Guitton Y. Histone content of germinating pea embryo chromatin decreases as DNA replicates. Nature. 1977;267(5613):724-6.
[13] Woodland HR. Histone synthesis during the development of Xenopus. FEBS Lett. 1980;121(1):1-10.
[14] Laskey RA, Honda BM, Mills AD, Finch JT. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature. 1978;275(5679):416-20.
[15] Mills AD, Laskey RA, Black P, De Robertis EM. An acidic protein which assembles nucleosomes in vitro is the most abundant protein in Xenopus oocyte nuclei. J Mol Biol. 1980;139(3):561-8.
[16] Nelson T, Hsieh TS, Brutlag D. Extracts of Drosophila embryos mediate chromatin assembly in vitro. Proc Natl Acad Sci U S A. 1979;76(11):5510-4.
[17] Nelson T, Wiegand R, Brutlag D. Ribonucleic acid and other polyanions facilitate chromatin assembly in vitro. Biochemistry. 1981;20(9):2594-601.
[18] Varshavskii AYa, Mikel'saar UN, Il'in YuV. Structure of chromatin deoxyribonucleoproteins. IV. Protein redistribution in the systems DNP-DNA, DNP-RNA, and DNP-DNP. Mol Biol. 1972;6(4):407-17.
[19] Gromov PS, Paponov VD, Sokolov NA et al. Structural chromatin modifications under the influence of polyanions. In the book.: Molecular mechanisms of genetic processes: Proc. of reports. III Proc. symposium. M., 1976, p. 47-48.
[20] Paponov VD, Gromov PS, Krasnov PA, Spitkovskii DM, Ruzga B. Dissociation and decompactization of chromatin by heparin in a medium of "physiologic" ionic strength. Biull Eksp Biol Med. 1980;90(9):325-8. ttp://
[21] Worcel A, Han S, Wong ML. Assembly of newly replicated chromatin. Cell. 1978;15(3):969-77.
[22] Earnshaw WC, Rekvig OP, Hannestad K. Histones synthesized for use in early development of Xenopus laevis are stored as a complex with antigenic properties similar to those of the octamer core of nucleosomes. J Cell Biol. 1982;92(3):871-6.
[23] Paponov VD, Gromov PS, Rupasov VV. Is the binding strength of histone fractions with DNA different? Biull Eksp Biol Med. 1980;90(8):163-5.
[24] Paponov VD, Gromov PS, Sokolov NA, Spitkovsky DM, Tseitlin PI. On mechanisms determining the interrelationships between DNA and histone components of chromatin. Eur J Biochem. 1980;107(1):113-22.