Biologia Plantarum

, Volume 55, Issue 1, pp 105–111 | Cite as

Combined drought and heat stress in wheat: changes in some heat shock proteins

Article

Abstract

The influence of combined and individually applied drought and heat stress was studied in two wheat (Triticum aestivum L.) cultivars: resistant cv. Katya and susceptible cv. Sadovo. Relative water content decreased and electrolyte leakage increased due to individual and combined application of both stresses. Initial heat shock protein profile has been outlined via SDS electrophoresis of leaf extracts. The results obtained were confirmed by immunoblotting with anti-HSP70 monoclonal antibodies, anti-HSP110 polyclonal antibodies and anti-α β-crystalline polyclonal antibodies. The effect of simultaneously applied water stress and heat shock resembled the alterations in protein expression provoked only by water stress and differed significantly from the changes occurring after the individual application of heat stress.

Additional key words

electrolyte leakage immunoblotting relative water content Triticum aestivum 

Abbreviations

D

drought stress

DH

combined drought and heat stress

EDTA

ethylendiaminetetracetic acid

H

heat stress

HSP

heat shock protein

PMSF

phenylmethanesulfonyl fluoride

RLS and RSS

Rubisco large and small subunits, respectively

SDS-PAGE

sodium dodecyl sulfate polyacrylamide gel electrophoresis

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Notes

Acknowledgements

This study was supported financially by the SCOPES program of the Swiss National Science Foundation (project DILPA-JRP-IB73AO-111142/1) and the Ministry of Education and Science of the Republic of Bulgaria (Contract No. CC1503). The authors are grateful to Dr. V. Vassileva for her assistance in the conductivity measurement analyses. They would also like to acknowledge the efforts of Dr. M. Stamenova who provided the α β-crystalline antibody. Thanks are extended to Mrs. B. Juperlieva- Mateeva, A. Kostadinova and I. Anders for their technical assistance.

References

  1. Barrs, H.D., Weatherley, P.E.: A re-examination of the relative turgidity technique for estimating water deficit in leaves. — Aust. J. biol. Sci. 15: 413–428, 1962.Google Scholar
  2. Bradford, M.M.: A rapid and sensitive method for the quantification of microgram quantities of proteins using the principle of protein-dye binding. — Anal. Biochem. 72: 248–254, 1976.CrossRefPubMedGoogle Scholar
  3. Caeiro, A.S., Ramos, P.C., Teixeira, A.R., Ferreira, R.B.: The ubiquitin/proteasome pathway from Lemna minor subjected to heat shock. — Biol. Plant. 52: 695–702, 2008.CrossRefGoogle Scholar
  4. Chaves, M.M., Oliveira, M.M.: Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture. — J. exp. Bot. 55: 2365–2384, 2004.CrossRefPubMedGoogle Scholar
  5. Demirevska, K., Simova-Stoilova, L., Vassileva, V., Feller, U.: Rubisco and some chaperone protein responses to water stress and rewatering at early seedling growth of drought sensitive and tolerant wheat varieties. — Plant Growth Regul. 56: 97–106, 2008.CrossRefGoogle Scholar
  6. Ferguson, B.: The plant response: stress in the daily environment. — J. Zhejiang Univ. Sci. 5: 129–132, 2004.CrossRefPubMedGoogle Scholar
  7. Geneva, M., Zehirov, G., Djonova, E., Kaloyanova, N., Georgiev, G., Strancheva, I.: The effect of inoculation of pea plants with mycorrhizal fungi and Rhizobium on nitrogen and phosphorus assimilation. — Plant Soil Environ. 52: 435–440, 2006.Google Scholar
  8. Gulli, M., Corradi, M., Rampino, P., Marmiroli, N., Perrotta, C.: Four members of the HSP101 gene family are differently regulated in Triticum durum Desf. — FEBS Lett. 581: 4841–4849, 2007.CrossRefPubMedGoogle Scholar
  9. Jiang, Y., Huang, B.: Protein alterations in tall fescue in response to drought stress and abscisic acid. — Crop Sci. 42: 202–207, 2002.CrossRefPubMedGoogle Scholar
  10. Kalapos, T., Van den Boogaard, R., Lambers, H.: Effect of soil drying on growth, biomass allocation and leaf gas exchange of two annual grass species. — Plant Soil 185: 137–149, 1996.CrossRefGoogle Scholar
  11. Kotak, S., Larkindale, J., Lee, U., Pascal von Koskull-Doring, Vierling, E., Scharf, K.: Complexity of the heat stress response in plants. — Plant Biol. 10: 310–316, 2007.Google Scholar
  12. Kregel, K.: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. — J. appl. Physiol. 92: 2177–2186, 2002.PubMedGoogle Scholar
  13. Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. — Nature 277: 680–685, 1970.CrossRefGoogle Scholar
  14. Lee, G., Vierling, E.: A small heat shock protein cooperates with heat shock protein 70 system to reactivate a heat-denaturated protein. — Plant Physiol. 122: 189–197, 2000.CrossRefPubMedGoogle Scholar
  15. Lee, U., Wie, C., Escobar, M., Williams, B., Hong, S., Vierling, E.: Genetic analysis reveals domain interactions of Arabidopsis HSP100/ClpB and cooperation with the small heat shock protein chaperone system. — Plant Cell 17: 559–571, 2005.CrossRefPubMedGoogle Scholar
  16. Lin, Q., Wang, Y.M., Nose, A., Hong, H.T.K., Agarie, S.: Effect of high night temperature on lipid and protein compositions in tonoplasts isolated from Ananas comosus and Kalanchoë pinnata leaves. — Biol. Plant. 52: 59–65, 2008.CrossRefGoogle Scholar
  17. Mansfield, M., Key, J.: Synthesis of the low molecular weight heat shock proteins in plants. — Plant Physiol. 84: 1007–1017, 1987.CrossRefPubMedGoogle Scholar
  18. Mayer, M., Bukau, B.: Hsp70 chaperones: cellular functions and molecular mechanism. — Cell Mol. Life Sci. 62: 670–684, 2005.CrossRefPubMedGoogle Scholar
  19. Miernyk, J.A.: Protein folding in the plant cell. — Plant Physiol. 121: 695–703, 1999.CrossRefPubMedGoogle Scholar
  20. Mitsuhashi, W., Feller, U.: Effects of light and external solutes on the catabolism of nuclear-encoded stromal proteins in intact chloroplasts isolated from pea leaves. — Plant Physiol. 100: 2100–2105, 1992.CrossRefPubMedGoogle Scholar
  21. Mittler, R.: Abiotic stress, the field environment and stress combination. — Trends Plant Sci. 11: 15–19, 2006.CrossRefPubMedGoogle Scholar
  22. Mittler, R., Merquiol, E., Hallak-Herr, E., Rachmilevitch, S., Kaplan, A., Cohen, M.: Living under a ‘dormant’ canopy: a molecular acclimation mechanism of the desert plant Retama raetam. — Plant J. 25: 407–416, 2001.CrossRefPubMedGoogle Scholar
  23. Moffat, A.S.: Finding new ways to protect drought-stricken plants. — Science 296: 1226–1229, 2002.CrossRefPubMedGoogle Scholar
  24. Nunes, M.E.S., Smith, G.R.: Electrolyte leakage assay capable of quantifying freezing resistance in rose clover. — Crop Sci. 43: 1349–1357, 2003.CrossRefGoogle Scholar
  25. Oh, H., Easton, D., Murawski, M., Kaneko, Y., Subjeck, J.: The chaperoning activity of HSP110. — J. biol. Chem. 274: 15712–15718, 1999.CrossRefPubMedGoogle Scholar
  26. Queitsch, C., Hong, S., Vierling, E., Lindquist, S.: Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. — Plant Cell 12: 479–492, 2000.CrossRefPubMedGoogle Scholar
  27. Rizhsky, L., Liang, H., Mittler, R.: The combined effect of drought stress and heat shock on gene expression in tobacco. — Plant Physiol. 130: 1143–1151, 2002.CrossRefPubMedGoogle Scholar
  28. Rizhsky, L., Liang, H., Shuman, J., Shulaev, V., Davletova, S., Mittler, R.: When defense pathways collide. The response of Arabidopsis to a combination of drought and heat stress. — Plant Physiol. 134: 1683–1696, 2004.CrossRefPubMedGoogle Scholar
  29. Ritossa, F.: A new puffing pattern induced by temperature shock and DNP in Drosophila. — Experientia 18: 571–573, 1962.CrossRefGoogle Scholar
  30. Santhoshkumar, P., Sharma, K.: Conserved F84 and P86 residues in αβ-crystallin are essential to effectively prevent the aggregation of substrate proteins. — Prot. Sci. 15: 2488–2498, 2006.CrossRefGoogle Scholar
  31. Santos, M.G., Ribeiro, R.V., Machado, E.C., Pimentel, C.: Photosynthetic parameters and leaf water potential of five common bean genotypes under mild water deficit. — Biol. Plant. 53: 229–236, 2009.CrossRefGoogle Scholar
  32. Schoffl, F., Prandl, R., Reindl, A.: Regulation of the heat-shock response. — Plant Physiol. 117: 1135–1141, 1998.CrossRefPubMedGoogle Scholar
  33. Simova-Stoilova, L., Vassileva, V., Demirevska, K., Feller, U.: Proteolytic activity in wheat leaves during drought stress and recovery. — Gen. Appl. Plant Physiol. 31(Spec. Issue): 91–100, 2006.Google Scholar
  34. Smykal, P., Masin, J., Hardy, I., Konopasek, I., Zarsky, V.: Chaperone activity of tobacco HSP18, a small heat-shock protein, is inhibited by ATP. — Plant J. 23: 703–713, 2000.CrossRefPubMedGoogle Scholar
  35. Sumesh, K.V., Sharma-Natu, P., Ghildiyal, M.C.: Starch synthase activity and heat shock protein in relation to thermal tolerance of developing wheat grains. — Biol. Plant. 52: 749–753, 2008.CrossRefGoogle Scholar
  36. Vierling, E.: The roles of heat shock proteins in plants. — Annu. Rev. Plant Physiol. Plant mol. Biol. 42: 579–620, 1991.CrossRefGoogle Scholar
  37. Wang, W., Vinocur, B., Shoseyov, O., Altman, A.: Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. — Trends Plant Sci. 9: 244–252, 2004.CrossRefPubMedGoogle Scholar
  38. Waters, E., Lee, G., Vierling, E.: Evolution, structure and function of the small heat shock proteins in plants. — J. exp. Bot. 47: 325–338, 1996.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • B. Grigorova
    • 1
  • I. Vaseva
    • 1
  • K. Demirevska
    • 1
  • U. Feller
    • 2
  1. 1.Institute of Plant PhysiologyBulgarian Academy of SciencesSofiaBulgaria
  2. 2.Institute of Plant Sciences and Oeschger Centre for Climate Change ResearchUniversity of BernBernSwitzerland

Personalised recommendations