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Expression of ‘dehydrin-like’ proteins in orthodox seeds of Ranunculus sceleratus during development and water stress

Published online by Cambridge University Press:  19 September 2008

G. E. Wechsberg ,
C. M. Bray  and
R. J. Probert
G. E. Wechsberg
Affiliation:
School of Biological Sciences, University of Manchester, Manchester, M13 9PT, UK Jodrell Laboratory, Royal Botanic Gardens, Kew, Wakehurst Place, Ardingly, West Sussex, RH17 6TN, UK
C. M. Bray
Affiliation:
School of Biological Sciences, University of Manchester, Manchester, M13 9PT, UK
R. J. Probert*
Affiliation:
Jodrell Laboratory, Royal Botanic Gardens, Kew, Wakehurst Place, Ardingly, West Sussex, RH17 6TN, UK
*
* Correspondence
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Abstract

Western blot analysis using antiserum raised against the lysine-rich box common to dehydrins, one class of late-embryogenesis-abundant (LEA) proteins, was used to study the abundance of heat-stable ‘dehydrin-like’ proteins during development and water stress in Ranunculus sceleratus L. achenes (seeds). A 61 kDa dehydrin-like protein was apparently limited to immature seeds (fresh and dried) which had not attained full desiccation tolerance. In contrast, lower-molecular-mass proteins which were induced by desiccation were found only in more mature seeds. The molecular masses of desiccation-induced proteins changed during seed development from 18 kDa in seeds harvested at 13 days post anthesis (DPA) to 31 kDa at harvest maturity, 21 DPA.

Placing seeds at 21 DPA in polyethylene glycol (PEG) at −1.5 MPa reduced seed moisture content and was accompanied by accumulation of 31 kDa protein. This protein was no longer detected when the seeds were transferred to water. In seeds harvested at 13 DPA, PEG induced the synthesis not only of 18 kDa protein (which is associated with dried seeds at this developmental stage), but also of 28 kDa and 31 kDa proteins. These dehydrin-like proteins were also synthesised when seeds at 13 DPA were imbibed in water. These and other data indicate that both quantitative and qualitative changes in dehydrin-like proteins can occur in R. sceleratus, depending on seed maturity and the degree and duration of water stress.

Keywords

dehydrindevelopmentlate-embryogenesis-abundant proteinsRanunculus sceleratus L.seedwater stress
Type
Short Communication
Information
Seed Science Research , Volume 4 , Issue 2 , June 1994 , pp. 241 - 246
Copyright
Copyright © Cambridge University Press 1994

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References

Baker, J.C., Steele, C. and Dure, L. III. (1988) Sequence and characterization of 6 LEA proteins and their genes from cotton. Plant Molecular Biology 11, 277–291.CrossRefGoogle ScholarPubMed
Blackman, S.A., Wettlaufer, S.H., Obendorf, R.L. and Leopold, A. C. (1991) Maturation proteins associated with desiccation tolerance in soybean. Plant Physiology 96, 868–874.CrossRefGoogle ScholarPubMed
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, 488–494.CrossRefGoogle ScholarPubMed
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, 95–108.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, 475–486.CrossRefGoogle ScholarPubMed
Espelund, M., Sæbøe-Larssen, S., Hughes, D.W., Galau, G.A., Larsen, F. and Jakobsen, K.S. (1992) Late embryogenesis-abundant genes encoding proteins with different numbers of hydrophilic repeats are regulated differentially by abscisic acid and osmotic stress. Plant Journal 2, 241–252.CrossRefGoogle ScholarPubMed
Galau, G.A., Hughes, D.W. and Dure, L. III (1986) Abscisic acid induction of cloned cotton late embryogenesisabundant (Lea) mRNAs. Plant Molecular Biology 7, 155–170.CrossRefGoogle ScholarPubMed
Hughes, D.W. and Galau, G.A. (1989) Temporally modular gene expression during cotyledon development. Genes and Development 3, 358–369.CrossRefGoogle ScholarPubMed
Kermode, A.R. (1990) Regulatory mechanisms involved in the transition from seed development to germination. Critical Reviews in Plant Science 9, 155–195.CrossRefGoogle Scholar
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Mundy, J. and Chua, N-H. (1988) Abscisic acid and water stress induce the expression of a novel rice gene. EMBO Journal 7, 2279–2286.CrossRefGoogle ScholarPubMed
Ooms, J.J.J., Léon-Kloosterziel, K.M., Bartels, D., Koornneef, M. and Karssen, C.M. (1993) Acquisition of desiccation tolerance and longevity in seeds of Arabidopsis thaliana. Plant Physiology 102, 1185–1191.CrossRefGoogle ScholarPubMed
Probert, R.J., Bogh, S.V., Smith, A.J. and Wechsberg, G.E. (1991) The effects of priming on seed longevity in Ranunculus sceleratus L. Seed Science Research 1, 243–249.CrossRefGoogle Scholar
Robertson, M. and Chandler, P.M. (1992) Pea dehydrins: identification, characterisation and expression. Plant Molecular Biology 19, 1031–1044.CrossRefGoogle Scholar
Skriver, K. and Mundy, J. (1990) Gene expression in response to abscisic acid and osmotic stress. Plant Cell 2, 503–512.Google ScholarPubMed
Wolfraim, L.A., Langis, R., Tyson, H. and Dhindsa, S. (1993) cDNA sequence, expression and transcript stability of a cold acclimation-specific gene, cas 18, of alfalfa (Medicago falcata) cells. Plant Physiology 101, 1257–1282.CrossRefGoogle Scholar