Plant and Cell Physiology Advance Access originally published online on January 17, 2006
Plant and Cell Physiology 2006 47(3):410-418; doi:10.1093/pcp/pcj008
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Control of the Synthesis and Subcellular Targeting of the Two GDH Genes Products in Leaves and Stems of Nicotiana plumbaginifolia and Arabidopsis thaliana
1 Laboratoire d’Androgénèse et Biotechnologie Végétale, Université de Picardie Jules Verne, 33, Rue saint-Leu, 80039 Amiens Cedex, France
2 Department of Genetics Anthropology Evolution, University of Parma, Parco Area delle Scienze 11/A, 43100 Parma, Italy
3 Department of Environmental Sciences, University of Parma, Parco Area delle Scienze 11/A, 43100 Parma, Italy
4 Unité de Nutrition Azotée des Plantes, Institut National de la Recherche Agronomique, R.D. 10, 78026 Versailles Cedex, France
* Corresponding author: E-mail, hirel{at}versailles.inra.fr; Fax, +33 1 30 83 30 96.
Although the physiological role of the enzyme glutamate dehydrogenase which catalyses in vitro the reversible amination of 2-oxoglutarate to glutamate remains to be elucidated, it is now well established that in higher plants the enzyme preferentially occurs in the mitochondria of phloem companion cells. The Nicotiana plumbaginifolia and Arabidopis thaliana enzyme is encoded by two distinct genes encoding either an 
- or a ß-subunit. Using antisense plants and mutants impaired in the expression of either of the two genes, we showed that in leaves and stems both the - and ß-subunits are targeted to the mitochondria of the companion cells. In addition, we found in both species that there is a compensatory mechanism up-regulating the expression of the -subunit in the stems when the expression of the ß-subunit is impaired in the leaves, and of the ß-subunit in the leaves when the expression of the -subunit is impaired in the stems. When one of the two genes encoding glutamate dehydrogenase is ectopically expressed, the corresponding protein is targeted to the mitochondria of both leaf and stem parenchyma cells and its production is increased in the companion cells. These results are discussed in relation to the possible signalling and/or physiological function of the enzyme which appears to be coordinated in leaves and stems.
5 These authors contributed equally to this work.
(Received November 8, 2005; Accepted January 5, 2006)
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