Plant Physiology Preview
Published on February 3, 2006; 10.1104/pp.105.074039
Received November 14, 2005
Returned for revision November 30, 2005
Accepted January 10, 2006
Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance
Julie Boudet , Julia Buitink , Folkert A. Hoekstra , Hélène Rogniaux , Colette Larré , Pascale Satour , and Olivier Leprince *
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, 16 boulevard Lavoisier, 49045 Angers, France
Laboratory of Plant Physiology, Department of Plant Sciences, Wageningen University, Arboretumlaan 4, 6703 BD Wageningen, The Netherlands
Unité de Recherche « Biopolymères, Interactions, Allergie » (Institut National de la Recherche Agronomique), rue de la Géraudière, BP 71624, 44316 Nantes
* Corresponding author; email: olivier.leprince{at}inh.fr.
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 re-induced, albeit that drought tolerance was increased. The abundance of 15 polypeptides was linked with DT, out of which 11 were identified as LEA 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 3 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 LEA proteins might exert different protective functions at high and low hydration levels.
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