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Manipulation of Glutathione and Amino Acid Biosynthesis in the Chloroplast1

Graham Noctor2, 3, *, Ana-Carolina M. Arisi2, Lise Jouanin, and Christine H. Foyer

Laboratoire du Métabolisme et de la Nutrition des Plantes (G.N.), and Laboratoire de Biologie Cellulaire (A.-C.M.A., L.J), Institut National de la Recherche Agronomique, 78026 Versailles cedex, France; and Institut National de la Recherche Agronomique, 78026 Versailles cedex, FranceDepartment of Environmental Biology, Institute of Grassland and Environmental Research, Plas Gogerddan, Ceredigion SY23 3EB, United Kingdom (G.N., C.H.F.)

Poplars (Populus tremula × Populus alba) were transformed to overexpress Escherichia coli gamma -glutamylcysteine synthetase (gamma -ECS) or glutathione synthetase in the chloroplast. Five independent lines of each transformant strongly expressed the introduced gene and possessed markedly enhanced activity of the gene product. Glutathione (GSH) contents were unaffected by high chloroplastic glutathione synthetase activity. Enhanced chloroplastic gamma -ECS activity markedly increased gamma -glutamylcysteine and GSH levels. These effects are similar to those previously observed in poplars overexpressing these enzymes in the cytosol. Similar to cytosolic gamma -ECS overexpression, chloroplastic overexpression did not deplete foliar cysteine or methionine pools and did not lead to morphological changes. Light was required for maximal accumulation of GSH in poplars overexpressing gamma -ECS in the chloroplast. High chloroplastic, but not cytosolic, gamma -ECS activities were accompanied by increases in amino acids synthesized in the chloroplast. We conclude that (a) GSH synthesis can occur in the chloroplast and the cytosol and may be up-regulated in both compartments by increased gamma -ECS activity, (b) interactions between GSH synthesis and the pathways supplying the necessary substrates are similar in both compartments, and (c) chloroplastic up-regulation of GSH synthesis is associated with an activating effect on the synthesis of specific amino acids formed in the chloroplast.

1   A.-C.M.A. was the recipient of a fellowship from Coordenaçao de Aperfeiçoamento de Pessoal de Ensino Superior, Ministry of Education, Brazil.
2   These authors contributed equally to the paper.
3   Present address: Department of Environmental Biology, Institute of Grassland and Environmental Research, Plas Gogerddan, Ceredigion SY23 3EB, UK.
*   Corresponding author; e-mail graham.noctor{at}bbsrc.ac.uk; fax 44-1970-828357.

Plant Physiol. (1998) 118: 471-482
Copyright Clearance Center:   0032-0889/98/118//12
© 1998 American Society of Plant Physiologists




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