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Stress protein content of mature Brassica seeds and their germination performance

Published online by Cambridge University Press:  19 September 2008

Mary Bettey*
Affiliation:
Horticulture Research International, Wellesbourne, Warwick, CV35 9EF, UK
W. E. Finch-Savage
Affiliation:
Horticulture Research International, Wellesbourne, Warwick, CV35 9EF, UK
*
*: Fax: 01789 470552 E-mail mary.bettey@hri.ac.uk

Abstract

Plants respond to sub-optimal conditions by the synthesis of specific ‘stress’ proteins, and these are thought to play a role in stress tolerance. Some of these proteins accumulate during late seed development, arguably to protect against damage during post-maturation drying and subsequent imbibition, prior to germination. Seed vigour is also determined during this late stage of seed development. High vigour seeds are those that can withstand the desiccation required for storage and successfully germinate under sub-optimal conditions to establish healthy seedlings. If stress proteins are involved in tolerating stress conditions, then they are likely to be important determinants of seed vigour. In this work the relationship between seed vigour (measured by seed germination performance following rapid aging, or under water stress) in Brassica oleracea var. capitata and the content of two classes of stress protein (dehydrins and a low molecular weight heat shock protein HSP17.6) at maturity was examined. Dehydrins did not show a positive relationship with seed performance. However, the protein HSP17.6 showed a positive correlation with seed performance, and a treatment that reduced the amount of this protein in the seed also caused a reduction in subsequent seed performance.

Type
Physiology & Biochemistry
Copyright
Copyright © Cambridge University Press 1998

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References

Baker, J., Steele, C. and Dure, L. III (1988) Sequence and characterization of 6 Lea proteins and their genes from cotton. Plant Molecular Biology 11, 277291.CrossRefGoogle ScholarPubMed
Bettey, M. and Finch-Savage, W.E. (1996) Respiratory enzyme activities during germination in Brassica seed lots of differing vigour. Seed Science Research 6, 165173.CrossRefGoogle Scholar
Blumenthal, C., Wrigley, C.W., Batey, I.L. and Barlow, E.W.R. (1994) The heat-shock response relevant to molecular and structural changes in wheat yield and quality. Australian Journal of Plant Physiology 21, 901909.Google Scholar
Bradford, K.J. and Chandler, P.M. (1992) Expression of “dehydrin-like” proteins in embryos and seedlings of Zizania palustris and Oryza sativa during dehydration. Plant Physiology 99, 488494.CrossRefGoogle ScholarPubMed
Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye-binding. Analytical Biochemistry 72, 248254.CrossRefGoogle Scholar
Bray, C.M. (1995) Biochemical processes during the osmopriming of seeds, pp 767789in Kigel, J., Galili, G. (Eds) Seed development and germination. New York, Marcel Dekker, Inc.Google Scholar
Close, T.J. (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiologia Plantarum 97, 795803.CrossRefGoogle Scholar
Close, T.J., Kortt, A.A. and Chandler, P.M. (1989) A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn. Plant Molecular Biology 13, 95108.CrossRefGoogle ScholarPubMed
Close, T.J., Fenton, R.D. and Moonan, F. (1993) A view of plant dehydrins using antibodies specific to the carboxy terminal peptide. Plant Molecular Biology 23, 279286.CrossRefGoogle Scholar
Dell'Aquila, A. and Taranto, G. (1986) Cell division and DNA-synthesis during osmopriming treatment and following germination in aged wheat embryos. Seed Science and Technology 14, 333341.Google Scholar
DeRocher, A.E. and Vierling, E. (1994) Developmental control of small heat shock protein expression during pea seed maturation. Plant Journal 5, 93102.CrossRefGoogle Scholar
DeRocher, A.E., Helm, K.W., Lauzon, L.M. and Vierling, E. (1991) Expression of a conserved family of cytoplasmic low molecular weight heat shock proteins during heat stress and recovery. Plant Physiology 96, 10381047.CrossRefGoogle ScholarPubMed
Dure, L. III, Crouch, M., Harada, J., Ho, T-H.D., Mundy, J., Quatrano, R., Thomas, T. and Sung, Z.R. (1989) Common amino acid sequence domains among the LEA proteins of higher plants. Plant Molecular Biology 12, 475486.CrossRefGoogle ScholarPubMed
Ellis, R.H. and Roberts, E.H. (1980) Improved equations for the prediction of seed longevity. Annals of Botany 45, 1330.CrossRefGoogle Scholar
Ferguson, I.B., Lurie, S. and Bowen, J.H. (1994) Protein synthesis and breakdown during heat shock of cultured pear (Pyrus communis L.) cells. Plant Physiology 104, 14291437.CrossRefGoogle ScholarPubMed
Finch-Savage, W.E. (1995) Influence of seed quality on crop establishment, growth and yield, pp 361384in Basra, A.S. (Ed.) Seed quality. Basic mechanisms and agricultural implications. Binghamton, NY, Haworth Press.Google Scholar
Fujikura, Y. and Karssen, C.M. (1992) Effects of controlled deterioration and osmopriming on protein synthesis of cauliflower seeds during early germination. Seed Science Research 2, 2331.CrossRefGoogle Scholar
Hampton, J.G. and Coolbear, P. (1990) Potential versus actual seed performance — can vigour testing provide an answer? Seed Science and Technology 18, 215228.Google Scholar
Hegarty, T.W. (1971) A relation between field emergence and laboratory germination in carrots. Journal of Horticultural Science 46, 299305.CrossRefGoogle Scholar
Helm, K.W. and Vierling, E. (1989) An Arabidopsis thaliana cDNA clone encoding a low molecular weight heat shock protein. Nucleic Acids Research 17, 7995.CrossRefGoogle ScholarPubMed
Helm, K.W., Petersen, N.S. and Abernethy, R.H. (1989) Heat shock response of germinating embryos of wheat. Plant Physiology 90, 598605.CrossRefGoogle ScholarPubMed
Houde, M., Danyluk, J., Laliberté, J.-F., Rassart, E., Dhindsa, R.S. and Sarhan, F. (1992) Cloning, characterization and expression of a cDNA encoding a 50-kilodalton protein specifically induced by cold acclimation in wheat. Plant Physiology 99, 13811387.CrossRefGoogle ScholarPubMed
ISTA (1993) International rules for seed testing. Seed Science and Technology 21, supplement.Google Scholar
Iturriaga, G., Schnieder, K., Salamini, F. and Bartels, D. (1992) Expression of desiccation-related proteins from the resurrection plant Craterostigma plantagineum in transgenic tobacco. Plant Molecular Biology 20, 555558.CrossRefGoogle ScholarPubMed
Jinn, T.-L., Chen, Y.-M., and Lin, C.-Y. (1995) Characterization and physiological function of class I low molecular mass, heat shock protein complex in soybean. Plant Physiology 108, 693701.CrossRefGoogle Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680685.CrossRefGoogle ScholarPubMed
Lanteri, S., Kraak, H.L., De Vos, C.H.R. and Bino, R.J. (1993) Effects of osmotic preconditioning on nuclear replication activity in seeds of pepper (Capsicum annuum). Physiologia Plantarum 89, 433440.CrossRefGoogle Scholar
Lee, G.J., Pokala, N. and Vierling, E. (1995a) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. Journal of Biological Chemistry 270, 1043210438.CrossRefGoogle ScholarPubMed
Lee, J.H., Hübel, A. and Schöffl, F. (1995b) Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant Journal 8, 603612.CrossRefGoogle ScholarPubMed
Lindquist, S. (1986) The heat shock response. Annual Review of Biochemistry 55, 11511191.CrossRefGoogle ScholarPubMed
Livesley, M.A. and Bray, C.M. (1993) Heat shock and recovery in aged wheat aleurone layers. Seed Science Research 3, 179186.CrossRefGoogle Scholar
Maude, R.B. (1996) Seedborne diseases and their control. Principles and practice. Wallingford, UK, CAB INTERNATIONAL.Google Scholar
Michel, B.E. (1983) Evaluation of the water potentials of solutions of polyethylene glycol 8000 both in the absence and presence of other solutes. Plant Physiology 72, 6670.CrossRefGoogle ScholarPubMed
Nguyen, H.T., Joshi, C.P., Klueva, N., Weng, J., Hendershot, K.L. and Blum, A. (1994) The heat-shock response and expression of heat-shock proteins in wheat under diurnal heat stress and field conditions. Australian Journal of Plant Physiology 21, 857867.Google Scholar
Parcy, F., Valon, C., Raynal, M., Gaubier-Comella, P., Delseny, M. and Giraudat, J. (1994) Regulation of gene expression programs during Arabidopsis seed development: roles of the ABI3 locus and of endogenous abscisic acid. Plant Cell 6, 15671582.Google ScholarPubMed
Perry, D.A. (1978) Report of the vigour test committee 1974–1977. Seed Science and Technology 6, 159181.Google Scholar
Prändl, R., Kloske, E. and Schöffl, F. (1995) Developmental regulation and tissue-specific differences of heat shock gene expression in transgenic tobacco and Arabidopsis plants. Plant Molecular Biology 28, 7382.CrossRefGoogle ScholarPubMed
Sanhewe, A.J., Ellis, R.H., Hong, T.D., Wheeler, T.R., Batts, G.R., Hadley, P. and Morison, J.I.L. (1996) The effect of temperature and CO2 on seed quality development in wheat (Triticum aestivum L.) Journal of Experimental Botany 47, 631637.CrossRefGoogle Scholar
Standard, S.A., Perret, D. and Bray, C.M. (1983) Nucleotide levels and loss of vigour and viability in germinating wheat embryos. Journal of Experimental Botany 34, 10471054.CrossRefGoogle Scholar
Steiner, J.J., Grabe, D.F. and Tulo, M. (1989) Single and multiple vigor tests for predicting seedling emergence of wheat. Crop Science 29, 782786.CrossRefGoogle Scholar
Still, D.W., Kovach, D.A. and Bradford, K.J. (1994) Development of desiccation tolerance during embryogenesis in rice (Oryza sativa) and wild rice (Zizania palustris). Plant Physiology 104, 431438.CrossRefGoogle ScholarPubMed
Trawatha, S.E., Steiner, J.J. and Bradford, K.J. (1990) Laboratory vigor tests used to predict pepper seedling field emergence performance. Crop Science 30, 713717.CrossRefGoogle Scholar
Vierling, E. (1991) The roles of heat shock proteins in plants. Annual Review of Plant Physiology and Plant Molecular Biology 42, 579620.CrossRefGoogle Scholar
Wehmeyer, N., Hernandez, L.D., Finkelstein, R.R. and Vierling, E. (1996) Synthesis of small heat shock proteins is part of the developmental program of late seed maturation. Plant Physiology 112, 747757.CrossRefGoogle ScholarPubMed
Xu, D., Duan, X., Wang, B., Hong, B., Ho, T-H.D. and Wu, R. (1996) Expression of a late embryogenesis abundant protein gene, HVA1, from barley confers tolerance to water deficit and salt stress in transgenic rice. Plant Physiology 110, 249257.CrossRefGoogle ScholarPubMed
Zarsky, V., Garrido, D., Eller, N., Tupy, J., Vicente, O., Schöffl, F. and Heberle-Bors, E. (1995) The expression of a small heat shock gene is activated during induction of tobacco pollen embryogenesis by starvation. Plant Cell and Environment 18, 139147.CrossRefGoogle Scholar
zur Nieden, U., Neumann, D., Bucka, A. and Nover, L. (1995) Tissue-specific localization of heat-stress proteins during embryo development. Planta 196, 530538.CrossRefGoogle Scholar