Plant Physiology Preview
Published on December 23, 2004; 10.1104/pp.104.052480
Received August 27, 2004
Returned for revision October 29, 2004
Accepted November 1, 2004
Identification in Pea Seed Mitochondria of a Late-Embryogenesis Abundant Protein Able to Protect Enzymes from Drying
Johann Grelet , Abdelilah Benamar , Emeline Teyssier , Marie-Hélène Avelange-Macherel , Didier Grunwald , and David Macherel *
Unité Mixte de Recherche 1191 Physiologie Moléculaire des Semences, Université d'Angers/INH/Institut National de la Recherche Agronomique, ARES, 49045 Angers cedex 01, France
Laboratoire Canaux Ioniques et Signalisation, Institut National de la Santé et de la Recherche Médicale EMI 9931, DRDC, Commissariat à l'Energie Atomique, 38054 Grenoble cedex 9, France
* Corresponding author; email: david.macherel{at}univ-angers.fr.
Late-embryogenesis abundant (LEA) proteins are hydrophilic proteins that accumulate to a high level in desiccation-tolerant tissues and are thus prominent in seeds. They are expected to play a protective role during dehydration; however, functional evidence is scarce. We identified a LEA protein of group 3 (PsLEAm) that was localized within the matrix space of pea (Pisum sativum) seed mitochondria. PsLEAm revealed typical LEA features such as high hydrophilicity and repeated motifs, except for the N-terminal transit peptide. Most of the highly charged protein was predicted to fold into amphiphilic  -helixes. PsLEAm was expressed during late seed development and remained in the dry seed and throughout germination. Application of the stress hormone abscisic acid was found to reinduce the expression of PsLEAm transcripts during germination. PsLEAm could not be detected in vegetative tissues; however, its expression could be reinduced in leaves by severe water stress. The recombinant PsLEAm was shown to protect two mitochondrial matrix enzymes, fumarase and rhodanese, during drying in an in vitro assay. The overall results constitute, to our knowledge, the first characterization of a LEA protein in mitochondria and experimental evidence for a beneficial role of a LEA protein with respect to proteins during desiccation.
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