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Etude de la globuline des graines de Tournesol (Helianthus annuus L.) accumulation au cours de la maturation et localisation intracellulaire

Study of sunflower (Helianthus annuus L.) seed globulin: Accumulation and intracellular localization

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Biologia Plantarum

Abstract

Protein synthesis and accumulation in growing sunflower (Helianthus annuus L.cv.Airelle) seeds are studied. The salt soluble fraction, globulin, is the main soluble protein component. The earlier stages of seed development (10 days after flowering) are characterized by high Mr polypeptides (74, 58 and 44 kDa). Later stages mainly show nature globulin polypeptides. Thus, protein synthesis in seed occurs at a specific period of seed development which follows a period of fast cell divisions (0–14 days after flowering). Protein bodies are isolated and their protein composition analyzed. Globulin subunits are the main polypeptides of protein bodies soluble fraction. Mature globulin is only stored in protein bodies.

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References

  • Adler, K., Müntz, K.: Origin and development of protein bodies in cotyledons ofVicia faba L. -Planta157: 401–410, 1983.

    Article  CAS  Google Scholar 

  • Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. - Anal. Biochem.72: 248–254, 1976.

    Article  PubMed  CAS  Google Scholar 

  • Dalgalarrondo, M., Raymond, J., Azanza, J. L.: Sunflower seed proteins: characterization and subunit composition of the globulin fraction. - J. exp. Bot.35: 1618–1628, 1984.

    Article  CAS  Google Scholar 

  • Donhowe, E. T., Peterson, D. M.: Isolation and characterization of oat aleurone layer and starchy endosperm protein bodies. - Plant Physiol.69: 148–155, 1982.

    Google Scholar 

  • Dure, L. S. III: Seed formation. - Annu. Rev. Plant Physiol.26: 259–278, 1975.

    Article  CAS  Google Scholar 

  • Ferjani, E.: Contribution à l’étude de la fraction protéique majeure (globuline) desgraines de Tournesol (Helianthus annuus L.). - Thèse de Doctorat d’Etatès Sciences. Pp. 219, Clermont-Ferrand (France), 1988.

  • Ferjani, E., Ledoigt, G.: Purification et caractérisation des polypeptides acides et basiques de la globuline de Tournesol. - Compt. rend. Soc. Biol.181: 624–632, 1987.

    CAS  Google Scholar 

  • Ferjani, E., Perrault, A., Ledoigt, G.: Precursor analysis and biosynthesis of sunflower globulin.- Plant Physiol. Biochem.27: 315–322, 1989.

    CAS  Google Scholar 

  • Greene, F. C.: Expression of storage protein genes in developing wheat (Triticum aestivum L.) seeds Correlation of RNA accumulation and protein synthesis. - Plant Physiol.71: 40–46, 1983.

    Article  PubMed  CAS  Google Scholar 

  • Higgins, T. J. V.: Synthesis and regulation of major proteins in seeds. - Annu. Rev. Plant Physiol.35: 191–221, 1984.

    Article  CAS  Google Scholar 

  • Laemmli, U. K.: Cleavage of structural proteins during the assembly of bacteriophage T4. - Nature227: 680–685, 1970.

    Article  PubMed  CAS  Google Scholar 

  • Pernollet, J. C.: Protein bodies of seeds: ultrastructure, biosynthesis and degradation. - Phytochemistry17: 1473–1480, 1978.

    Article  CAS  Google Scholar 

  • Pernollet, J. C.: Biosynthesis and accumulation of storage proteins in seeds. - Physiol. vég.23: 45–59, 1985.

    CAS  Google Scholar 

  • Plant, A. R., Moore, K. G.: NADH cytochrome c-reductase activity associated with a membrane fraction from protein bodies ofLupinus angustifolius cotyledons. - New Phytol.93: 359–368, 1983.

    Article  CAS  Google Scholar 

  • Psaras, G.: The structure of sunflower (Helianthus annuus) endosperm during germination. - Phytomorphology35: 141–146, 1985.

    Google Scholar 

  • Pusztai, A., Stewart, J. C., Watt, W. B.: A novel method for the preparation of protein bodies by filtration in high (over 70 % w/v) sucrose-containing media. - Plant Sci. Lett.12: 9–15, 1978.

    Article  CAS  Google Scholar 

  • Sabir, M. A., Sosulski, F. W., Mac Kenzie, S. L.: Gel chromatography of sunflower proteins. -J. agr. Food Chem.21: 988–993, 1973.

    Article  CAS  Google Scholar 

  • Schwenke, K. D., Raab, B.: The distribution of the protein fractions obtained from sunflower seeds. -Nährung17: 373–379, 1973.

    Article  PubMed  CAS  Google Scholar 

  • This, P., Goffner, D., Raynal, M., Charter, Y., Delseny, M.: Characterization of major storage proteins of sunflower and their accumulation. - Plant Physiol. Biochem.26: 125–132, 1988.

    CAS  Google Scholar 

  • Tully, R. E., Beevers, H.: Protein bodies of castor bean endosperm. - Plant Physiol.58: 710–716, 1976.

    PubMed  CAS  Google Scholar 

  • Weber, E., Neumann, D.: Protein bodies, storage organelles in plant seeds. - Biochem. Physiol. Pflanz.175: 279–306, 1980.

    CAS  Google Scholar 

Download references

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Authors and Affiliations

  1. Ecole Normale supérieure, 70121, Bizerte, Tunisie

    E. Ferjani

  2. Laboratoire de Phytomorphogenése UA 45 C.N.R.S., Biologie et Physiologie Végétales, Université Clermont II, 4 rue Ledru, 63038, Clermont-Ferrand, France

    G. Ledoigt

Authors
  1. E. Ferjani
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  2. G. Ledoigt
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Ferjani, E., Ledoigt, G. Etude de la globuline des graines de Tournesol (Helianthus annuus L.) accumulation au cours de la maturation et localisation intracellulaire. Biol Plant 32, 429–435 (1990). https://doi.org/10.1007/BF02890889

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  • DOI: https://doi.org/10.1007/BF02890889

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