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Molecular Biology Reports

, Volume 13, Issue 4, pp 191–196 | Cite as

Comparative filter binding study of H5 to nucleosome core particles, H1, H5 depleted chromatosomes and DNA fragments

  • S. Pennings
  • S. Muyldermans
  • L. Wyns
Article

Abstract

The filter-binding technique with PEI treated glass fiber is used to study the interaction of histone H5 to core particles, chromatosomes and DNA derived from it. By working at very low concentrations of interacting particles we are able to study the effective binding process independent of interfering insoluble complexes. The interactions are characterized by a very high affinity. An intrinsically higher affinity of H5 for cores and chromatosomes versus chromatosome derived DNA is demonstrated. Both chromatosomes and DNA derived from these bind about twice the amount as compared to core particles, which saturate at about one H5 per core particle.

Key words

chromatosome histone H5 lattice binding nucleosome core particles 

Abbreviations

GH5

globular domain of histone H5

PEI

polyethyleneimine

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References

  1. 1.
    Simpson RT (1978) Biochemistry 17: 5524–5531Google Scholar
  2. 2.
    Aviles F, Chapman G, Kneale G, Crane-Robinson C & Bradbury M (1978) Eur. J. Biochem. 88: 363–371Google Scholar
  3. 3.
    Allan J, Hartman PG, Crane-Robinson C & Aviles FX (1980) Nature 288: 675–679Google Scholar
  4. 4.
    Allan J, Mitchell T, Harnborne N, Bohm L & Crane-Robinson C (1986) J. Mol. Biol. 187: 591–601Google Scholar
  5. 5.
    Bates DL & Thomas JO (1981) Nucl. Acids Res. 9: 5883–5894Google Scholar
  6. 6.
    Ali Z & Singh N (1978) J. Biol. Chem. 262: 12989–12993Google Scholar
  7. 7.
    Watanabe F (1986) Nucl. Acids Res. 14: 3575–3585Google Scholar
  8. 8.
    Bruns RF, Lawson-Wendling K & Pugsley TA (1983) Anal. Biochem. 132: 74–81Google Scholar
  9. 9.
    Muyldermans S, Lasters I, Wyns L & Hamers R (1981) Nucl. Acids Res., 9: 3671–3680Google Scholar
  10. 10.
    Pennings S, Muyldermans S & Wyns L (1986) Biochemistry 25: 5043–5051Google Scholar
  11. 11.
    Glazer AN, Delange RJ & Sigman DS (1982) in Chemical Modifications of proteins. Work & Work, eds, ElsevierGoogle Scholar
  12. 12.
    McGhee JD & Von Hippel PH (1974) J. Mol. Biol. 86: 469–489Google Scholar
  13. 13.
    Epstein IR (1978) Biophys. Chem. 8: 327–329Google Scholar
  14. 14.
    Schreier AA & Schimmel PR (1974) J. Mol. Biol. 86: 601–620Google Scholar
  15. 15.
    Clark DJ & Thomas JO (1986) J. Mol. Biol. 187: 569–580Google Scholar
  16. 16.
    Clark DJ & Thomas JO (1988) Eur. J. Biochem. 178: 225–233Google Scholar

Copyright information

© Kluwer Academic Publishers 1989

Authors and Affiliations

  • S. Pennings
    • 1
  • S. Muyldermans
    • 1
  • L. Wyns
    • 1
  1. 1.Laboratory of General BiologyFree UniversitySint-Genesius-RodeBelgium

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