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ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance^1,[W]

Unité Mixte de Recherche 1191, Physiologie Moléculaire des Semences (Université d'Angers, Institut National d'Horticulture, Institut National de la Recherche Agronomique), Anjou Recherche Semences, 49045 Angers, France (J. Boudet, J. Buitink, P.S., O.L.); Laboratory of Plant Physiology, Department of Plant Sciences, Wageningen University, 6703 BD Wageningen, The Netherlands (F.A.H.); and Unité de Recherche, Biopolymères, Interactions, Allergie, Institut National de la Recherche Agronomique, 44316 Nantes, France (H.R., C.L.)

A proteomic analysis was performed on the heat stable protein fraction of imbibed radicles of Medicago truncatula seeds to investigate whether proteins can be identified that are specifically linked to desiccation tolerance (DT). Radicles were compared before and after emergence (2.8 mm long) in association with the loss of DT, and after reinduction of DT by an osmotic treatment. To separate proteins induced by the osmotic treatment from those linked with DT, the comparison was extended to 5 mm long emerged radicles for which DT could no longer be reinduced, albeit that drought tolerance was increased. The abundance of 15 polypeptides was linked with DT, out of which 11 were identified as late embryogenesis abundant proteins from different groups: MtEm6 (group 1), one isoform of DHN3 (dehydrins), MtPM25 (group 5), and three members of group 3 (MP2, an isoform of PM18, and all the isoforms of SBP65). In silico analysis revealed that their expression is likely seed specific, except for DHN3. Other isoforms of DNH3 and PM18 as well as three isoforms of the dehydrin Budcar5 were associated with drought tolerance. Changes in the abundance of MtEm6 and MtPM25 in imbibed cotyledons during the loss of DT and in developing embryos during the acquisition of DT confirmed the link of these two proteins with DT. Fourier transform infrared spectroscopy revealed that the recombinant MtPM25 and MtEm6 exhibited a certain degree of order in the hydrated state, but that they became more structured by adopting helices and sheets during drying. A model is presented in which DT-linked late embryogenesis abundant proteins might exert different protective functions at high and low hydration levels.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Olivier Leprince (olivier.leprince{at}inh.fr).

^[W] The online version of this article contains Web-only data.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.074039.

^* Corresponding author; e-mail olivier.leprince{at}inh.fr; fax 33–2–41–22–55–49.

Received November 14, 2005; returned for revision January 8, 2006; accepted January 10, 2006.

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