Hostname: page-component-76fb5796d-r6qrq Total loading time: 0 Render date: 2024-04-25T14:15:24.769Z Has data issue: false hasContentIssue false
  • English
  • Français

Developmental pattern of biotinylated proteins during embryogenesis and maturation of soybean seed1

Published online by Cambridge University Press:  19 September 2008

José B. França Neto ,
Robert G. Shatters Jr  and
S. H. West
José B. França Neto*
Affiliation:
USDA/ARS at the University of Florida, Agronomy Seed Laboratory, P.O. Box 110770, Gainesville, FL 32611–0770, USA
Robert G. Shatters Jr
Affiliation:
USDA/ARS at the University of Florida, Agronomy Seed Laboratory, P.O. Box 110770, Gainesville, FL 32611–0770, USA
S. H. West
Affiliation:
USDA/ARS at the University of Florida, Agronomy Seed Laboratory, P.O. Box 110770, Gainesville, FL 32611–0770, USA
*
*correspondence
Get access Rights & Permissions [Opens in a new window]

Abstract

The developmental pattern of biotinylated proteins (BP) during embryogenesis and maturation of soybean seed was characterized. Detection of these BP was compared with the development of desiccation tolerance in seeds. Three groups of BP were detected in soybean seeds using a biotin-streptavidin detection method: the first group consisted of a set of three bands with a mean apparent MW of 85 kDa (called BP85), detected in crude extracts of embryonic axes (EA) from non-dehydrated seeds (NDS) and from artificially slow-dehydrated seeds (DS); the second one, BP75, was a single protein with an apparent MW of 75 kDa and was expressed in cotyledons (COT) and EA tissues of NDS and DS; the third group with a mean apparent MW of 35 kDa (BP35), was expressed at high levels only in COT of NDS. BP35 concentration was highest in the early stages of seed development (21 days after flowering — DAF) and decreased as seeds developed, being almost imperceptible after 47 DAF. Conversely, only traces of BP75 and BP85 extracted from EA and COT were detected at early stages of seed development (21–33 DAF). Maximum levels of accumulation of these proteins were expressed at 42–47 DAF and remained constant until harvest maturity. Desiccation-tolerant stage of the seeds was initiated at 47 DAF, which coincided with the stage of maximum accumulation of BP75 and BP85 in the seeds, however, appearance of these proteins could be stimulated by desiccation of immature seeds that had not achieved desiccation tolerance. Therefore changes in biotinylated proteins are coincident with, but not sufficient for, the development of desiccation tolerance.

Keywords

SoybeanGlycine maxbiotinbiotinylated proteinseed developmentdesiccation
Type
Physiology and Biochemistry
Information
Seed Science Research , Volume 7 , Issue 4 , December 1997 , pp. 377 - 384
Copyright
Copyright © Cambridge University Press 1997

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.)

Footnotes

2

Research funded by USDA-ARS, Embrapa-Brazilian Corporation for Agricultural Research and CNPq-Conselho Nacional de Desenvolvimento Científico e Technológico, Brazil

References

Anderson, J.W. and Beardall, J. (1991) Enzymes and post-translational enzyme regulation. pp 61–82in Anderson, J.W. (Ed.) Molecular activities of plant cells — an introduction to plant biochemistry. Oxford, Blackwell Scientific Publications.Google Scholar
Andrews, C.H. (1966) Some aspects of pod and seed development in Lee soybeans. PhD Thesis. Mississippi State University, Mississippi State.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
Bartels, D., Singh, M. and Salamini, F. (1988) Onset of desiccation tolerance during development of the barley embryo. Planta 175, 485–492.CrossRefGoogle ScholarPubMed
Bender, A.E. (1982) Dicionário de nutrição e tecnologia de alimentos (Dictionary of nutrition and food technology), 4th edition, São Paulo, Livraria Roca Ltda.Google Scholar
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
Blackman, S.A., Obendorf, R. and Leopold, A.C. (1992) Maturation proteins and sugars in desiccation tolerance of developing soybean seeds. Plant Physiology 100, 225–230.CrossRefGoogle ScholarPubMed
Boo, S.P. (1995) Characterization of molecular events that occur during soybean (Glycine max) seed germination. MSc Thesis. University of Florida, Gainesville.Google Scholar
Boo, S.P., West, S.H., Sasser, J.A., França Neto, J.B. and Shatters, R.G. Jr (1995) Immunological identification of a novel putative late embryogenic abundant protein in soybean seeds (Abstract No. 468). Plant Physiology 108, S–96Google Scholar
Bradford, M.M. (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle Scholar
Dehaye, L., Job, C., Duval, M. and Job, D. (1996) Developmental and biochemical features of LEA protein from Pisum sativum L., SBP65, which binds biotin as a prosthetic group (abstract No. 151). Plant Physiology 111, S–58.Google Scholar
Dakshinamurti, K. and Bhagavan, N.H. (1985) Biotin. Annals of the New York Academy of Sciences 447, 1–441.Google ScholarPubMed
Dure, L. III, Crouch, M., Harada, J., Ho, T.D., Mundy, J., Quatrano, R., Thomas, T. and Sung, Z.R. (1989) Common amino acid sequence domains among LEA proteins of higher plants. Plant Molecular Biology 12, 475–486.CrossRefGoogle ScholarPubMed
Duval, M., DeRose, R.T., Job, C., Faucher, D., Douce, R. and Job, D. (1994a) The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site. Plant Molecular Biology 26, 265–273.CrossRefGoogle Scholar
Duval, M., Job, C., Alban, C., Douce, R. and Job, D. (1994b) Development patterns of free and protein-bound biotin during maturation and germination of seeds of Pisum sativum: Characterization of a novel seed-specific biotinylated protein. Journal of Biochemistry 299, 141–150.CrossRefGoogle ScholarPubMed
Fehr, W.R. and Caviness, C.E. (1977) Stages of soybean development. Special Report 80, Cooperative Extension Service, Iowa State University, Ames.Google Scholar
Harrington, J.F. (1972) Seed storage and longevity. pp 145–245in Kozlowski, T.T. (Ed.) Seed biology. Vol 3. New York, Academic Press.Google Scholar
Hendry, G.A.F. (1993) Oxygen, free radical processes and seed longevity. Seed Science Research 3, 141–153.CrossRefGoogle Scholar
Hoppe, H.H. and Zacher, H. (1985) Inhibition of fatty acid biosynthesis in isolated bean and maize chloroplasts by herbicidal phenoxy-phenoxypropionic acid derivatives and structurally related compounds. Pesticide Biochemistry and Physiology 24, 298–305.CrossRefGoogle Scholar
Horbowicz, M. and Obendorf, R.L. (1994) Seed desiccation tolerance and storability: dependence of flatulence-producing oligosaccharides and cyclitols — review and survey. Seed Science Research 4, 385–405.CrossRefGoogle Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680–685.Google Scholar
Leprince, O., Bronchart, R. and Deltour, R. (1990) Changes in starch and soluble sugars in relation to the acquisition of desiccation tolerance during maturation of Brassica campestris seed. Plant Cell and Environment 13, 539–546.CrossRefGoogle Scholar
Leprince, O., Hendry, G.A.F. and McKersie, B.D. (1993) The mechanisms of desiccation tolerance in developing seeds. Seed Science Research 3, 231–246.CrossRefGoogle Scholar
Mitchell, H.H. (1950) Nutritive factors in soybean products. pp 383–422in Marklet, K.S. (Ed.) Soybeans and soybean products, Vol. 1, New York, Interscience Publishers, Inc.Google Scholar
Quebedeaux, B., Sweetser, P.B. and Rowell, J.C. (1976) Abscisic acid levels in soybean reproductive structures during development. Plant Physiology 58, 363–366.CrossRefGoogle ScholarPubMed
Rosenberg, L.A. and Rinne, R.W. (1988) Protein synthesis during natural and precocious soybean seed (Glycine max [L.] Merr.) maturation. Plant Physiology 87, 474–478.CrossRefGoogle ScholarPubMed
Shatters, R.G., Boo, S.P., França Neto, J.B. and West, S.H. (1997) Identification of biotinylated proteins in soybean (Glycine max L.) seeds and their characterization during germination and seedling growth. Seed Science Research 7, 373–376.CrossRefGoogle Scholar
Schneider, T.R., Dinkins, R., Robinson, K., Shellhamer, J. and Meinke, D.W. (1989) An embryo-lethal mutant of Arabidopsis thaliana is a biotin auxotroph. Developmental Biology 131, 161–167.CrossRefGoogle ScholarPubMed
White, A., Handler, P. and Smith, E.L. (1973) The water soluble vitamins. pp 1152–1183in Brehem, J.J., Stryker-Rodda, A. (Eds) Principles of biochemistry, Ed 5. New York, McGraw-Hill, Inc.Google Scholar
Wijeratne, W.B. (1991) Composition of soybean. pp 9–25in Tanteeratarm, K. (Ed.) Soybean processing for food uses, Urbana, Illinois, INTSOY, University of Illinois.Google Scholar
Wurtele, E.S. and Nikolau, B.J. (1990). Plants contain multiple biotin enzymes: discovery of 3-methylcrotonyl-CoA carboxylase, propionyl-CoA carboxylase and pyruvate carboxylase in the plant kingdom. Archives of Biochemistry and Biophysics 278, 179–186.CrossRefGoogle ScholarPubMed