Advertisement

Proteins from the Prokaryotic Nucleoid: Biochemical and 1H NMR Studies on Three Bacterial Histone-Like Proteins

  • M. Lammi
  • M. Paci
  • C. L. Pon
  • M. A. Losso
  • A. Miano
  • R. T. Pawlik
  • G. L. Gianfranceschi
  • C. O. Gualerzi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 179)

Abstract

In the past, the absence of histones and organized chromatin were regarded as characteristics of the prokaryotic cell. In reality, the approximately 4000 kb circular chromosome of bacteria is condensed in a region called the nucleoid and gentle lysis methods allowed the obtainment of chromatin-like fibers with repetitive granular structure. The granules have a diameter ≃ 130 Å and are reminiscent of the eukaryotic nucleosome (1). In the structural organization of “bacterial chromatin”, a role is probably played by specific DNA-binding proteins (2–5). Only recently, the characterization of the structural and functional properties of these proteins has been undertaken in various laboratories.

Keywords

Hydrophobic Region Hydrophilic Region Strong Hydrophobic Interaction Dimeric Interaction Selective Chemical Modification 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Griffith, J.D. (1976) Proc. Natl. Acad. Sci. USA 73, 563.PubMedCrossRefGoogle Scholar
  2. 2.
    Rouviere-Yaniv, J. and Gros, F. (1975) Proc. Natl. Acad. Sci. USA 72, 3428.PubMedCrossRefGoogle Scholar
  3. 3.
    Berthold, V. and Geider, K. (1976) Eur. J. Biochem. 71, 443.PubMedCrossRefGoogle Scholar
  4. 4.
    Varshavsky, A.J., Nedospasov, S.A., Bakayeva, V.V. and Georgiev, G.P. (1977) Nucleic Acids Res. 4, 2725.PubMedCrossRefGoogle Scholar
  5. 5.
    Geider, K. and Hoffmann-Berling, H. (1981) Annu. Rev. Biochem. 50, 233.PubMedCrossRefGoogle Scholar
  6. 6.
    Suryanarayana, T. and Subramanian, A.R. (1978) Biochim. Biophys. Acta 520, 342.PubMedCrossRefGoogle Scholar
  7. 7.
    Lathe, R., Buc, H., Lecocq, J-P. and Bautz, E.K.F. (1980) Proc. Natl. Acad. Sci. USA 77, 3548.PubMedCrossRefGoogle Scholar
  8. 8.
    Spassky, A. and Buc, H.C. (1977) Eur. J. Biochem. 81, 79.PubMedCrossRefGoogle Scholar
  9. 9.
    Dijk, J., White, S.W., Wilson, K.S. and Appelt, K. (1983) J. Biol. Chem. 258, 4003.PubMedGoogle Scholar
  10. 10.
    Gianfranceschi, G.L., Amici, D. and Guglielmi, L. (1975) Biochim. Biophys. Acta 414, 9.PubMedCrossRefGoogle Scholar
  11. 11.
    Miano, A., Losso, M.A., Gianfranceschi, G.L. and Gualerzi, C.O. (1982) Biochem. Internat. 5, 415.Google Scholar
  12. 12.
    Losso, M.A., Miano, A., Gianfranceschi, G.L. and Gualerzi, C.O. (1982) Biochem. Internat. 5, 423.Google Scholar
  13. 13.
    Paci, M., Pon, C.L., Losso, M.A. and Gualerzi, C.O. (1983) in press.Google Scholar
  14. 14.
    Mende, L., Timm, B. and Subramanian, A.R. (1978) FEBS Lett. 96, 395.PubMedCrossRefGoogle Scholar
  15. 15.
    Kyte, J. and Doolittle, R.F. (1982) J. Mol. Biol. 157, 105.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • M. Lammi
    • 2
  • M. Paci
    • 1
  • C. L. Pon
    • 1
  • M. A. Losso
    • 2
  • A. Miano
    • 3
  • R. T. Pawlik
    • 1
  • G. L. Gianfranceschi
    • 3
  • C. O. Gualerzi
    • 3
  1. 1.Abt. WittmannMax-Planck-Institut für Molekulare GenetikBerlinGermany
  2. 2.Dept. of Cell BiologyUniversity of CalabriaCalabria (CS)Italy
  3. 3.Dept. of Cell BiologyUniversity of CamerinoCamerino (MC)Italy

Personalised recommendations