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First published online September 11, 2003; 10.1104/pp.103.025254

Plant Physiology 133:664-682 (2003)
© 2003 American Society of Plant Biologists

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DEVELOPMENT AND HORMONE ACTION

Proteomics of Medicago truncatula Seed Development Establishes the Time Frame of Diverse Metabolic Processes Related to Reserve Accumulation1

Karine Gallardo*, Christine Le Signor, Joël Vandekerckhove, Richard D. Thompson and Judith Burstin

Unité de Génétique et Ecophysiologie des Légumineuses, Institut National de la Recherche Agronomique (INRA)-Dijon, Domaine d'Epoisses, 21110 Bretenières, France (K.G., C.L.S., R.D.T., J.B); and Flanders Interuniversity Institute for Biotechnology and Department of Biochemistry, Gent University, Gent, Belgium (J.V.)

We utilized a proteomic approach to investigate seed development in Medicago truncatula, cv Jemalong, line J5 at specific stages of seed filling corresponding to the acquisition of germination capacity and protein deposition. One hundred twenty proteins differing in kinetics of appearance were subjected to matrix-assisted laser desorption ionization time of flight mass spectrometry. These analyses provided peptide mass fingerprint data that identified 84 of them. Some of these proteins had previously been shown to accumulate during seed development in legumes (e.g. legumins, vicilins, convicilins, and lipoxygenases), confirming the validity of M. truncatula as a model for analysis of legume seed filling. The study also revealed proteins presumably involved in cell division during embryogenesis ({beta}-tubulin and annexin). Their abundance decreased before the accumulation of the major storage protein families, which itself occurs in a specific temporal order: vicilins (14 d after pollination [DAP]), legumins (16 DAP), and convicilins (18 DAP). Furthermore, the study showed an accumulation of enzymes of carbon metabolism (e.g. sucrose synthase, starch synthase) and of proteins involved in embryonic photosynthesis (e.g. chlorophyll a/b binding), which may play a role in providing cofactors for protein/lipid synthesis or for CO2 refixation during seed filling. Correlated with the reserve deposition phase was the accumulation of proteins associated with cell expansion (actin 7 and reversibly glycosylated polypeptide) and of components of the precursor accumulating vesicles, which give rise to a trypsin inhibitor on maturation. Finally, we revealed a differential accumulation of enzymes involved in methionine metabolism (S-adenosyl-methionine synthetase and S-adenosylhomo-cysteine hydrolase) and propose a role for these enzymes in the transition from a highly active to a quiescent state during seed development.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.025254.

1 This work was supported by the INRA-Action Transversale Structurante program on Medicago truncatula and by INRA (postdoctoral fellowship to K.G.).

* Corresponding author; e-mail gallardo{at}epoisses.inra.fr; fax 33–3–80–69–32–63.

Received April 30, 2003; returned for revision May 27, 2003; accepted July 1, 2003.




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