First published online May 25, 2007; 10.1105/tpc.107.050104
The Plant Cell 19:1580-1589 (2007)
© 2007 American Society of Plant Biologists
Structure and Function of a Mitochondrial Late Embryogenesis Abundant Protein Are Revealed by Desiccation[W]
Dimitri Tolletera,
Michel Jaquinodb,
Cécile Mangavelc,
Catherine Passiranid,
Patrick Saulnierd,
Stephen Manone,
Emeline Teyssiera,
Nicole Payeta,
Marie-Hélène Avelange-Macherela and
David Macherela,1,2
a Unité Mixte de Recherche 1191, Physiologie Moléculaire des Semences, Université d'Angers/Institut National d'Horticulture/Institut National de la Recherche Agronomique, Angers F-49045, France
b Commissariat à l'Energie Atomique, Département des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, Laboratoire d'Etude de la Dynamique des Protéomes, Institut National de la Santé et de la Recherche Médicale, Equipe de Recherche Méthodologique 0201, Grenoble F-38054, France
c Unité de Recherche Biopolymères Interactions Assemblages, Institut National de la Recherche Agronomique, Nantes F-44316, France
d Institut National de la Santé et de la Recherche Médicale U646, Université d'Angers, Angers F-49100, France
e Institut de Biochimie et Génétique Cellulaires, Unité Mixte de Recherche 5095, Bordeaux F-33077, France
2 To whom correspondence should be addressed. E-mail dmbio{at}nivabio.org; fax 33-241-225-549.
Few organisms are able to withstand desiccation stress; however, desiccation tolerance is widespread among plant seeds. Survival without water relies on an array of mechanisms, including the accumulation of stress proteins such as the late embryogenesis abundant (LEA) proteins. These hydrophilic proteins are prominent in plant seeds but also found in desiccation-tolerant organisms. In spite of many theories and observations, LEA protein function remains unclear. Here, we show that LEAM, a mitochondrial LEA protein expressed in seeds, is a natively unfolded protein, which reversibly folds into  -helices upon desiccation. Structural modeling revealed an analogy with class A amphipathic helices of apolipoproteins that coat low-density lipoprotein particles in mammals. LEAM appears spontaneously modified by deamidation and oxidation of several residues that contribute to its structural features. LEAM interacts with membranes in the dry state and protects liposomes subjected to drying. The overall results provide strong evidence that LEAM protects the inner mitochondrial membrane during desiccation. According to sequence analyses of several homologous proteins from various desiccation-tolerant organisms, a similar protection mechanism likely acts with other types of cellular membranes.
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