Control of the synthesis and subcellular targeting of the two GDH genes products in leaves and stems of Nicotiana plumbaginifolia and Arabidopsis thaliana.
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 alpha- or a beta-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 alpha- and beta-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 alpha-subunit in the stems when the expression of the beta-subunit is impaired in the leaves, and of the beta-subunit in the leaves when the expression of the alpha-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.
Fontaine
Jean-Xavier
JX
Laboratoire d'Androgénèse et Biotechnologie Végétale, Université de Picardie Jules Verne, Amiens, France.
Saladino
Francesca
F
Agrimonti
Caterina
C
Bedu
Magali
M
Tercé-Laforgue
Thérèse
T
Tétu
Thierry
T
Hirel
Bertrand
B
Restivo
Francesco M
FM
Dubois
Frédéric
F
D016375:Antisense Elements (Genetics); D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D035264:Flowers / Q000648:ultrastructure; D015870:Gene Expression; D018506:Gene Expression Regulation, Plant; D005969:Glutamate Dehydrogenase / Q000096:biosynthesis* / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D009154:Mutation / Q000235:genetics; D009243:NAD / Q000378:metabolism; D018515:Plant Leaves / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D010940:Plant Proteins / Q000378:metabolism; D018547:Plant Stems / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D030821:Plants, Genetically Modified; D021381:Protein Transport; D014026:Nicotiana / Q000201:enzymology* / Q000235:genetics
D016375:Antisense Elements (Genetics); D007527:Isoenzymes; D010940:Plant Proteins; D009243:NAD; D005969:Glutamate Dehydrogenase