Histone Methylation and Modulation of Gene Expression in Response to Heat Shock and Chemical Stress in Drosophila

  • Robert M. Tanguay
  • Richard Desrosiers
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)


All prokaryotic and eukaryotic organisms examined respond to an exposure to supraoptimal temperatures or to various forms of cellular stress by the rapid induction of a small set of proteins, the heat shock proteins 1–3. In Drosophila where this response was originally observed, extensive gene regulation has been shown to operate at the transcriptional and post-transchptional levels4. In this system, the rapid activation of the heat shock genes observed at the puff level is accompanied by an equally rapid repression of the transcription of most of the genes active prior to the shock (referred to hereafter as the normal genes). The molecular mechanisms involved in the rapid induction or repression of specific genes in response to stress are still unclear.


Heat Shock Methylation Pattern Histone Methylation Core Histone Heat Shock Gene 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    B.G. Atkinson and D.B. Waiden (Eds), “Changes In Eukaryotic Gene Expression in Response to Environmental Stress”, Academic Press, Orlando (1985).Google Scholar
  2. 2.
    L. Nover (Ed.), “Heat Shock Response of Eukaryotic Cells”, VEB Georg Thieme, Leipzig (1984).Google Scholar
  3. 3.
    S. Lindquist, The heat-shock response, Ann. Rev. Biochem .55: 1151 (1986)PubMedCrossRefGoogle Scholar
  4. 4.
    R.M. Tanguay, Genetic regulation during heat shock and function of heat-shock proteins: a review, Can. J. Biochem. Cell Biol .61: 387 (1983).PubMedCrossRefGoogle Scholar
  5. 5.
    R.S. Wu, H.T. Panusz, C.L. Hatch and W.M. Bonner, Histones and their modifications. CRC Crit. Rev. Biochem .20: 201 (1986)PubMedCrossRefGoogle Scholar
  6. 6.
    R. Camato and R.M. Tanguay, Changes in the methylation pattern of core histones during heat shock in Drosophila cells, EMBO J .1: 1529 (1982).PubMedGoogle Scholar
  7. 7.
    A. P. Arrigo, Acetylation and methylation patterns of core histones are modified after heat or arsenite treatment of Drosophila tissue culture cells, Nucleic Acids Res .11:1389 (1983).PubMedCrossRefGoogle Scholar
  8. 8.
    R. Desrosiers and R.M. Tanguay, The modifications in the methylation patterns of H2B and H3 after heat shock can be correlated with the inactivation of normal gene expression, Biochem. Biophys. Res. Commun., 133: 823 (1985).PubMedCrossRefGoogle Scholar
  9. 9.
    R. Desrosiers and R.M. Tanguay, Further characterization of the posttranslational modifications of core histones in response to heat and arsenite stress in Drosophila, Biochem. Cell Biol .64: 750 (1986).Google Scholar
  10. 10.
    W.K. Paik and S. Kim, “Protein Methylation” John Wiley & Sons, New-York (1980).Google Scholar
  11. 11.
    M. Vincent and R.M. Tanguay, Different intracellular distribution of heat-shock and arsenite-induced proteins in Drosophila Kc cells, J. Mol. Biol .162: 365 (1982).PubMedCrossRefGoogle Scholar
  12. 12.
    J.O. Thomas and R.D. Kornberg, An octamer of histones in chromatin and free in solution, Proc. Natl. Acad. Sci. USA 72: 2626 (1975).PubMedCrossRefGoogle Scholar
  13. 13.
    R.C. Findly and T. Pederson, Regulated transcription of the genes for actin and heat-shock proteins in cultured Drosophila cells, J. Cell Biol .88: 323 (1981).PubMedCrossRefGoogle Scholar
  14. 14.
    R. Zandomeni and R. Weinmann, Inhibitory effect of 5,6-DichIoro-l-ß-D-ribofuranosylbenzimidazole on a protein kinase, J. Biol. Chem .259: 14804 (1984)PubMedGoogle Scholar
  15. 15.
    A. Martinage, G. Briand, A. Van Dorsselaer, C.H. Turner and P. Sautière, Primary structure of histone H2B from gonads of the starfish Asterias rubens. Eur. J. Biochem .147: 351 (1985).PubMedCrossRefGoogle Scholar
  16. 16.
    P. Byvoet and C.S. Baxter, Histone methylation, a functional enigma, in “Chromosomal Proteins and their Role in the Regulation of Gene Expression”, G.S. Stein and L.V. Kleinsmith, eds., Academic Press, New-York(1975).Google Scholar
  17. 17.
    A. Hershko, H. Heller, E. Eytan, G. Kaklij and I.A. Rose, Role of the α-amino group of protein in ubiquitin-mediated protein breakdown, Proc. Natl. Acad. Sci. USA. 81: 7021 (1984).PubMedCrossRefGoogle Scholar
  18. 18.
    A. Bachmair, D. Finley and A. Varshavsky, In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179 (1986)PubMedCrossRefGoogle Scholar
  19. 19.
    H.A. Parag, B. Raboy and R.G. Kulka, Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system, EMBO J .6:55(1987).PubMedGoogle Scholar
  20. 20.
    G.W. Pettigrew and G.M. Smith, Novel N-terminal protein blocking group identified as dimethylproline, Nature 265: 661 (1977).PubMedCrossRefGoogle Scholar
  21. 21.
    N. Carlson, S. Rogers and M. Rechsteiner, Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock, J. Cell Biol., 104: 547(1987).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Robert M. Tanguay
    • 1
  • Richard Desrosiers
    • 1
  1. 1.Ontogénèse et Génétique MoléculairesCentre Hospitalier de l’Université LavalSte-FoyCanada

Personalised recommendations