Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-10T20:15:56.356Z Has data issue: false hasContentIssue false
  • English
  • Français

Isolation and characterization of a heat-soluble protein from pea (Pisum sativum) embryos

Published online by Cambridge University Press:  19 September 2008

Pauline S. Russouw ,
Jill Farrant ,
Wolf Brandt ,
Dennis Maeder  and
George G. Lindsey
Pauline S. Russouw
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, RONDEBOSCH 7700, South Africa
Jill Farrant
Affiliation:
Department of Botany, University of Cape Town, Private Bag, RONDEBOSCH 7700, South Africa
Wolf Brandt
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, RONDEBOSCH 7700, South Africa
Dennis Maeder
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, RONDEBOSCH 7700, South Africa
George G. Lindsey*
Affiliation:
Department of Biochemistry, University of Cape Town, Private Bag, RONDEBOSCH 7700, South Africa
*
*Correspondence
Get access Rights & Permissions [Opens in a new window]

Abstract

An LEA-like protein has been isolated and characterized from pea (Pisum sativum) embryos. It is the most prevalent protein in a homogenate of pea axes heated for 10 min at 80°C and then centifuged for 10 min at 17000 g (80°C supernatant fraction). It has a molecular mass of 11 kDa and is very rich in hydrophilic amino acids, notably aspartate, glutamate and glycine. The protein is not recognized by an antibody to the group II dehydrin C-terminal consensus sequence. Antibodies to the isolated protein recognize a number of larger proteins in the 80°C supernatant fraction of pea and other legumes (chick pea, soybean and bean) as well as gramineous seeds (wheat, maize and barley). The protein undergoes a substantial increase in α-helical content at high ionic strength but does not dimerize.

Keywords

DesiccationLEA proteinpea embryosprotein characterization
Type
Physiology and Biochemistry
Information
Seed Science Research , Volume 5 , Issue 3 , September 1995 , pp. 137 - 144
Copyright
Copyright © Cambridge University Press 1995

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Almoguera, C. and Jordano, J. (1992) Developmental and concurrent expression of sunflower dry-seed-stored low molecular weight heat-shock protein and LEA mRNAs. Plant Molecular Biology 19, 781–792.Google Scholar
Atherton, E. and Sheppard, R.C. (1989) Solid phase peptide synthesis: a practical approach. Oxford, I.R.L. Press.Google Scholar
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, 277–291.CrossRefGoogle ScholarPubMed
Bewley, J.D. and Black, M. (1985) Seeds. Physiology of development and germination. New York, London, Plenum Press.Google Scholar
Bewley, J.D. and Oliver, M.J. (1992) Desiccation tolerance in vegetative plant tissues and seeds: protein synthesis in relation to desiccation and a potential role for protection and repair mechanisms. pp 141–160 in Somero, G.N., Osmond, C.B. and Bosix, C.L. (Eds) Water and Life: Comparative analysis of water relationships at the organismic, cellular and molecular levels. Berlin, Springer-Verlag.CrossRefGoogle Scholar
Bray, E.A. (1993) Molecular responses to water deficit. Plant Physiology 103, 1035–1040.Google Scholar
Ceccardi, T.L., Meyer, N.C. and Close, T.J. (1994) Purification of a Maize dehydrin. Protein Expression and Purification 5, 1–4.CrossRefGoogle ScholarPubMed
Close, T.J. and Lammers, P. (1993) An osmotic stress protein of cyanobacteria is immunologically related to plant dehydrin. Plant Physiology 101, 773–779.Google Scholar
Close, T.J., Kort, 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
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, 279–286.Google Scholar
Curry, J., Morris, C.F. and Walker-Simmons, M.K. (1991) Sequence analysis of a cDNA encoding a Group 3 LEA mRNA inducible by ABA or dehydration in wheat. Plant Molecular Biology 16, 1073–1076.Google Scholar
Dure, L. III, (1993) A repeating 11-mer amino acid sequence domains among the LEA proteins of higher plants. Plant Journal 3, 363–369.Google Scholar
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
Finch-Savage, W.E., Pramanik, S.K. and Bewley, J.D. (1994) The expression of dehydrin proteins in desiccation-sensitive (recalcitrant) seeds of temperate trees. Planta 193, 478–485.Google Scholar
Galau, G.A. and Close, T.J. (1992) Sequences of the cotton Group 2 LEA/RAB/dehydrin proteins encoded by LEA 3 cDNA's. Plant Physiology 98, 1523–1525.CrossRefGoogle Scholar
Galau, G.A., Hughes, D.W. and Dure, L. III, (1986)Abscisic acid induction of cloned cotton late embryogenesis-abundant (lea) mRNA's. Plant Molecular Biology 7, 157–170.Google Scholar
Gee, O.H., Probert, R.J. and Coomber, S.A. (1994) ‘Dehydrin-like’ proteins and desiccation tolerance in seeds. Seed Science Research 4, 135–141.Google Scholar
Harlow, E. and Lane, D. (1988) Antibodies — A laboratory manual. Cold Spring Harbour Laboratory.Google Scholar
Hennessy, J.P. and Johnson, W.C. (1981) Information content in the circular dichroism of proteins. Biochemistry 20, 1085–1094.CrossRefGoogle Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227, 680–685.Google Scholar
Lottspeich, F. (1985) Micro-scale isocratic separation of the phenylthiohydantin amino acid derivatives. Journal of Chromatography 326, 321–327.Google Scholar
McManus, M.T., McKeating, J., Secher, D.S., Osborne, D.J., Ashford, D., Dwek, R.A. and Rademacher, T.W. (1988) Identification of a monoclonal antibody to abscission tissue that recognises xylose/fucose-containing N-linked oligosaccharides from higher plants. Planta 175, 506–512.Google Scholar
O'Farrell, P.H. (1975) High resolution two- dimensional electrophoresis of proteins. Journal of Biological Chemistry 250, 4007–4021.Google Scholar
Oullet, F., Houde, M. and Sarhan, F. (1993) Purification, characterisation and c-DNA cloning of a 200 kDa protein induced by cold acclimation in wheat. Plant Cell Physiology 34, 59–65.Google Scholar
Piatkowski, D., Schneider, K., Salamini, F. and Bartels, D. (1990) Characterization of five abscisic acid-resposive cDNA clones isolated from the desiccation-tolerant plant Craterostigma plantagineum and their relationship to other water-stress genes. Plant Physiology 94, 1682–1688.CrossRefGoogle ScholarPubMed
Reid, J.L. and Walker-Simmons, M.K. (1993) Group 3 Late embryogenesis abundant proteins in desiccation tolerant seedlings of wheat (Triticum aestivum L.). Plant Physiology 102, 125–131.Google Scholar
Robertson, M. and Chandler, P.M. (1992) Pea dehydrins: identification, characterisation and expression. Plant Molecular Biology 19, 1031–1044.Google Scholar
Saxena, V.P. and Wetlaufer, D.B. (1971) A new basis for interpreting the circular dichroic spectra of proteins. Proceedings of the National Academy of Sciences, USA 66, 969–972.Google Scholar
Skriver, K. and Mundy, J. (1990) Gene expression in response to abscisic acid and osmotic stress. Plant Cell 2, 503–512.Google Scholar
Vertucci, C.W. and Farrant, J.M. (1994) Acquisition and loss of desiccation tolerance. pp 237–271 in Kigel, J. and Galili, G. (Eds). Seed development and germination. New York, Marcel Dekker Inc.Google Scholar