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Genetic diversity for seed protein composition in Medicago truncatula

Published online by Cambridge University Press:  12 February 2007

C. Le Signor ,
K. Gallardo ,
J.M. Prosperi ,
C. Salon ,
L. Quillien ,
R. Thompson  and
G. Duc
C. Le Signor*
Affiliation:
Unité de recherche en génétique et écophysiologie des légumineuses, BP 86510, F21065Dijon Cedex
K. Gallardo
Affiliation:
Unité de recherche en génétique et écophysiologie des légumineuses, BP 86510, F21065Dijon Cedex
J.M. Prosperi
Affiliation:
UMR-DGPC Station de génétique et d'amélioration des plantes INRA, Domaine de Melgueil, F34130Mauguio
C. Salon
Affiliation:
Unité de recherche en génétique et écophysiologie des légumineuses, BP 86510, F21065Dijon Cedex
L. Quillien
Affiliation:
Unité de biochimie et technologie des protéines, INRA, F44316 Nantes Cedex 03, France
R. Thompson
Affiliation:
Unité de recherche en génétique et écophysiologie des légumineuses, BP 86510, F21065Dijon Cedex
G. Duc
Affiliation:
Unité de recherche en génétique et écophysiologie des légumineuses, BP 86510, F21065Dijon Cedex
*
*Corresponding author: E-mail:, [email protected]
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Abstract

Fifty lines of Medicago truncatula, derived from ecotypes or cultivars of diverse geographical origin, were grown under uniform conditions, and variation in seed protein composition and quantity was investigated. One-dimensional electrophoretic profiles revealed 46 major seed polypeptides, of which 26 were polymorphic within the collection. The vicilin/convicilin (7S) and the legumin (11S) type proteins were identified by immunoblotting using antibodies raised against the homologous pea proteins. The polymorphism for the major seed protein classes allowed the clustering of the genotypes into four groups. There was no evidence of clustering according to geographical origin of the lines. However, all lines not belonging to either M. truncatula ssp. truncatula or ssp. longispina were clustered in a single group, demonstrating the value of seed protein profiles in delimiting species boundaries. The Jemalong line group was differentiated early in the dendrogram, and thus represents an ancient clade in the seed diversity of M. truncatula. Within-accession variation was investigated for one-dimensional seed profiles, with additional lines obtained from the same ecotypes. As expected for an autogamous species, within-accession variation was low. Seed protein content was highly variable among the 50 lines examined. Lines contrasting for qualitative traits and seed protein content were identified to allow for the genetic determination of these characters.

Keywords

ecotypeelectrophoresisgenetic variationimmunoblottingMedicago truncatulaseed protein content
Type
Research Article
Information
Plant Genetic Resources , Volume 3 , Issue 1 , April 2005 , pp. 59 - 71
Copyright
Copyright © NIAB 2005

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References

Allen, SE (1974) Chemical Analysis of Ecological Materials. New YorkJohn Wiley and Sons.Google Scholar
Bastianelli, D, Grosjean, F, Peyronnet, C, Duparque, M and Régnier, JM (1998) Feeding value of pea (Pisum sativum L.). 1. Chemical composition of different categories of pea. Animal Science 67: 609–619.CrossRefGoogle Scholar
Bena, G, Prosperi, JM, Lejeune, B and Olivieri, I (1998) Evolution of annual species of the genus Medicago: a molecular phylogenetic approach. Molecular Phylogenetics and Evolution 9: 552–559.CrossRefGoogle ScholarPubMed
Bertozo, MR and Valls, JFM (2001) Seed storage protein electrophoresis in Arachis pintoi and A. repens (Leguminosae) for evaluating genetic diversity. Genetic Ressources and Crop Evolution 48: 121–130.CrossRefGoogle Scholar
Bewley, JD and Black, M (1994) Seeds: Physiology of Development and Germination, 2nd edn. New York: Plenum Press.CrossRefGoogle Scholar
Blum, H, Beier, H and Gross, HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8: 93–99.CrossRefGoogle Scholar
Bradford, MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Analytical Biochemistry 72: 248–254.CrossRefGoogle ScholarPubMed
Brown, WM, George, M and Wilson, AC (1979) Rapid evolution of animal mitochondrial DNA. Proceedings of the National Academy of Science USA 76: 1967–1971.CrossRefGoogle ScholarPubMed
Croy, RRD and Gatehouse, JA (1985) Genetic engineering of seed proteins: current and potential application. In: Dodds, JH (ed.) Plant Genetic Engineering Cambridge: Cambridge University Press, pp. 143–268.Google Scholar
Duc, G (2004) Seed composition of Medicago truncatula (line J5), compared to other seed legumes. Proceedings of the Fifth European Conference on Grain Legumes with the Second International Conference on Legume Genomics and Genetics, AEP-ICLGG 2004,2004, 11–7 June,Dijon, France, pp. 404.Google Scholar
Gallardo, K, Job, C, Groot, SPC, Puype, M, Demol, H, Vandekerckhove, J and Job, D (2002 a) Importance of methionine biosynthesis for Arabidopsis seed germination and seedling growth. Plant Physiology 126: 238–247.CrossRefGoogle Scholar
Gallardo, K, Job, C, Groot, SPC, Puype, M, Demol, H, Vandekerckhove, J and Job, D (2002 b) Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds. Plant Physiology 129: 823–837.CrossRefGoogle ScholarPubMed
Gallardo, K Le, Signor, C, Vandekerckhove, J, Thompson, RD and Burstin, J (2003) Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation. Plant Physiology 133: 1–19.CrossRefGoogle ScholarPubMed
Gueguen, J, Vu, AT and Schaeffer, F (1984) Large scale purification and characterization of pea globulins. Journal of the Science of Food and Agriculture 35: 1024–1033.CrossRefGoogle Scholar
Hoffman, B, Trinh, TH, Leung, J, Kondorosi, A and Kondorosi, E (1997) A new Medicago truncatula line with superior in vitro regeneration, transformation, and symbiotic properties isolated through cell culture selection. Molecular Plant–Microbe Interactions 10: 307–315.CrossRefGoogle Scholar
Krochko, JE and Bewley, JD (1988) Use of electrophoretic techniques in determining the composition of seed storage proteins in alfafa. Electrophoresis 9: 751–763.CrossRefGoogle Scholar
Krochko, JE and Bewley, JD (2000) Seed storage proteins in cultivars and subspecies of alfafa (Medicago sativa). Seed Science Research 10: 423–434.CrossRefGoogle Scholar
Ladizinsky, G and Hymowitz, T (1979) Seed protein electrophoresis in taxonomic and evolutionary studies. Theoretical and Applied Genetics 54: 145–151.CrossRefGoogle ScholarPubMed
Laemmli, UK (1970) Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227: 680–685.CrossRefGoogle ScholarPubMed
Mathesius, U, Keijzers, G, Natera, SH, Weinman, JJ, Djordjevic, MA and Rolfe, BG (2001) Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics 1: 1424–1440.3.0.CO;2-J>CrossRefGoogle ScholarPubMed
Mishra, SK, Sharma, B, Dasgupta, SK and Mathur, N (2000) Variations in electrophoretic patterns of storage seed proteins in pea (Pisum sativum). Annals of Agricultural Research 21: 405–409.Google Scholar
Payne, PI (1983) Breeding for protein quantity and protein quality in seed crops. In: Daussant, J, Mossé, J and Vaughan, J (eds) Seed Proteins, Annual Proceedings of the Phytochemical Society of Europe No. 20. London: Academic Press, pp. 223–253.Google Scholar
Perrot, C (1995) Les protéines de pois: de leur fonction dans la graine à leur utilisation en alimentation animale. INRA Productions Animales 8: 151–164.CrossRefGoogle Scholar
Potokina, E and Eggi, E (1997) Intraspecific diversity of Vicia sativa L. and Vicia angustifolia Reichard deduced from seed protein electrophoresis. FABIS Newsletter 40: 13–17.Google Scholar
Sagan, M, De Larembergue, H and Morandi, D, et al. (1998) Genetic analysis of symbiosis mutants in Medicago trucatula. In: Emerich, C (ed.) Biological Nitrogen Fixation for the 21st Century. Dordrecht: Kluwer Academic Publishers, pp. 317–318.CrossRefGoogle Scholar
SAS Institute Inc. (1990) SAS/STAT User's Guide, Version 6, 4th edn. Cary, NC: SAS Institute pp. 893–997.Google Scholar
Schroeder, HE (1982) Quantitative studies on the cotyledonary proteins in the genus Pisum. Journal of the Science of Food and Agriculture 33: 623–633.CrossRefGoogle ScholarPubMed