Do Antarctic Fish Respond to Heat Shock?

  • Luisella Carratù
  • Andrew Y. Gracey
  • Stefania Buono
  • Bruno Maresca


Temperature is a major environmental factor requiring adaptive responses and it is a central selective element in speciation. One of the best known and complex mechanisms that is primarily involved in protecting cells from various forms of stresses, such as temperature, is the stress (heat shock) response [1], For poikilotherms, fluctuations in environmental temperatures can be fatal. Sudden drops in temperature can lead to a reduction in membrane fluid state that, in turn, causes cessation of normal functions. Unless rapidly corrected, such alterations will lead to physiological damage and, ultimately, to death. Several essential cellular activities depend on proper membrane functionality [2]. For elevated environmental temperatures, some of the problems encountered during chilling are also relevant. There still exist the dual needs of being able to “sense” the elevated environmental temperature and to couple this detection to the induction of gene expression — such as for heat shock genes. Recently, there have been several lines of evidence which suggest that changes in response to an abrupt rise in the environmental temperature may have analogies with chilling adaptation. Thus, membrane lipid composition, as well as the dynamic state of membrane lipids, represent the basic elements for membrane functionality. Membranes, indeed, have multiple physical properties which permit the cell to sense environmental changes.


Heat Shock Heat Shock Response Heat Shock Factor Heat Shock Transcription Factor Heat Shock Gene 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Lindquist S, Craig EA (1988) The heat shock proteins. Ann Rev Genet 22: 631–677PubMedCrossRefGoogle Scholar
  2. 2.
    Cossins AR, Bowler K (1987) Temperature biology of animals. Chapman & Hall, New YorkCrossRefGoogle Scholar
  3. 3.
    Carratù L, Franceschelli S, Pardini CL, Kobayashi GS, Horvath I, Vigh L, Maresca B (1996) Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast. Proc Natl Acad Sci USA 93: 2120–2125Google Scholar
  4. 4.
    Vigh L, Los DA, Horwath I, Murata N (1993) The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desk gene in Synechocystis PCC6803. Proc Natl Acad Sci USA 90: 9090–9094PubMedCrossRefGoogle Scholar
  5. 5.
    Hegner D (1980) Age-dependence of molecular and functional changes in biological membrane properties. Mech Ageing Dev 12: 207–214Google Scholar
  6. 6.
    Dimri GP, Campisi J (1994) Altered profile of transcription factor-binding activities in senescent human fibroblasts. Exp Cell Res 212: 116–124CrossRefGoogle Scholar
  7. 7.
    Mejia R, Gomez Eichelmann MC, Fernandez MS (1995) Membrane fluidity of Escherichia coli during heat-shock. Biochim Biophys Acta 1223: 195–200Google Scholar
  8. 8.
    Revathi CJ, Chattopadhyay A, Srinivas UK (1994) Change in membrane organization induced by heat shock. Biochem Mol Biol Int 16: 925–950Google Scholar
  9. 9.
    Eastman JT (1993) Antarctic fish biology. Evolution in unique environment. Academic Press, San DiegoGoogle Scholar
  10. 10.
    Somero GS (1991) Biochemical mechanisms of cold adaptation and stenothermality in Antarctic fish. In: di Prisco G, Maresca B, Tota B (eds) Biology of Antarctic fish. Springer-Verlag, Heidelberg, pp 216–231Google Scholar
  11. 11.
    Maresca B, Patriarca E, Goldenberg C, Sacco M (1988) Heat shock and cold adaptation in Antarctic fishes: a molecular approach. Comp Biochem Physiol 90B: 623–614Google Scholar
  12. 12.
    Freeman BC, Myers MP, Schumacher R, Morimoto RI (1995) Identification of a regulatory motif in HSP70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 14: 2131–2142Google Scholar
  13. 13.
    Bienz M, Pelham HRB (1987) Mechanisms of heat-shock gene activation in higher eukaryotes. Advances in Genetics 24: 31–72PubMedCrossRefGoogle Scholar
  14. 14.
    Lis J, Wu C (1993) Protein traffic on the heat shock promoter: parking, stalling, and trucking along. Cell 74: 1–4PubMedCrossRefGoogle Scholar
  15. 15.
    Pelham HRB, Bienz M (1982) A synthetic heat shock promoter element confers heat inducibility on the herpes simplex virus thymidine kinase gene. EMBO J 1: 1313–1317Google Scholar
  16. 16.
    Xiao H, Lis JT (1988) Germline transformation used to define key features of the heat shock response element. Science 223: 1123–1126Google Scholar
  17. 17.
    Amin J, Ananthan J, Voellmy R (1988) Key features of heat shock regulatory elements. Mol Cell Biol 8: 2161–2169Google Scholar
  18. 18.
    Perisic O, Xiao H, Lis JT (1989) Stable binding of Drosophila heat shock factor to head-to-head and tail-to-tail repeats of a conserved 5 bp recognition unit. Cell 59: 797–806PubMedCrossRefGoogle Scholar
  19. 19.
    Xiao H, Perisic O, Lis JT (1991) Cooperative binding of Drosophila heat shock factor to arrays of a conserved 5 bp unit. Cell 64: 585–593PubMedCrossRefGoogle Scholar
  20. 20.
    Kroeger PE, Sarge KD, Morimoto RI (1993) Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element. Mol Cell Biol 13: 1610–1623Google Scholar
  21. 21.
    Bienz M, Pelham HRB (1986) Heat shock regulatory elements function as an inducible enhancer in Xenopus hsp70 gene and when linked to a heterologous promoter. Cell 14: 753–760CrossRefGoogle Scholar
  22. 22.
    Chen J, Pederson DS (1993) A distal heat shock element promotes the rapid response to heat shock of the hsp26 gene in the yeast Saccharomyces cerevisiae. J Biol Chem 268: 7132–7122Google Scholar
  23. 23.
    Amin J, Fernandez M, Ananthan J, Lis JT, Voellmy R (1994) Cooperative binding of heat shock transcription factor to the hsp70 promoter in vivo and in vitro. J. Biol. Chem 269: 1604–1611Google Scholar
  24. 24.
    Cohen RS, Meselson M (1988) Periodic interactions of heat shock transcriptional elements. Nature 172: 856–858CrossRefGoogle Scholar
  25. 25.
    Lewin B (1994) Genes V. Oxford University PressGoogle Scholar
  26. 26.
    Langford CJ, Klniz FJ, Donath C, Gallwitz D (1984) Point mutations identify the conserved intron-contained TACTAAC box as an essential splicing signal sequence in yeast. Cell 20: 614–653Google Scholar
  27. 27.
    Marchler G, Schüller C, Adam G, Ruis H (1993) A Saccharomyces cerevisiae UAS element controlled by protein kinase A activates transcription in response to a variety of stress conditions. EMBO J 12: 1997–2003PubMedGoogle Scholar
  28. 28.
    Mager WH, Kruijff AJJ (1995) Stress-induced transcriptional activation. Microb Reviews 5: 506–531Google Scholar
  29. 29.
    Somero GN, DeVries AL (1967) Temperature tolerance of some Antarctic fishes. Science 156: 257–258PubMedCrossRefGoogle Scholar
  30. 30.
    Harrison P, Gargano S, Maresca B (1989) Physical analysis and regulation of the gene hsp70 in Antarctic fish. Scienza e Cultura. Proceedings of the 1st meeting on “Biology in Antarctica”Google Scholar
  31. 31.
    Morimoto RI, Kroeger PE, Cotto JJ (1996) The transcriptional regulation of heat shock genes: a plethora of heat shock factors and regulatory conditions. In: Feige U, Morimoto RI, Yahara I, Polla BS (eds) Stress-inducible cellular responses. Birkhauser Verlag, Basel Boston Berlin. pp 123–163Google Scholar
  32. 32.
    Nakai A, Morimoto RI (1993) Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway. Mol Cell Biol 13: 1983–1997PubMedGoogle Scholar

Copyright information

© Springer-Verlag Italia 1998

Authors and Affiliations

  • Luisella Carratù
    • 1
  • Andrew Y. Gracey
    • 2
  • Stefania Buono
    • 1
  • Bruno Maresca
    • 1
  1. 1.International Institute of Genetics and BiophysicsCNRNapoliItaly
  2. 2.Department of Environmental and Evolutionary BiologyUniversity of LiverpoolLiverpoolUK

Personalised recommendations