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PLANT PHYSIOLOGY , Vol 101, Issue 2 561-566, Copyright © 1993 by American Society of Plant Biologists
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METABOLISM AND ENZYMOLOGY |
Localization of [gamma]-Glutamylcysteine Synthetase and Glutathione Synthetase Activity in Maize Seedlings
A. Ruegsegger and C. Brunold
Pflanzenphysiologisches Institut der Universitat Bern, Altenbergrain 21, CH-3013 Bern, Switzerland
Fresh weight, protein, cysteine, [gamma]-glutamylcysteine, glutathione, and
the extractable activity of the enzymes of glutathione biosynthesis,
[gamma]-glutamylcysteine synthetase (EC 6.3.2.2) and glutathione synthetase
(EC 6.3.2.3), were measured in roots, scutella, endosperms, and shoots of
3-, 7-, and 11-d-old maize (Zea mays L. cv LG 9) seedlings. In 3-d-old
seedlings, the scutella represented 14% of the seedling fresh weight,
containing 43% of total protein and 63 and 55% of the activity of
[gamma]-glutamylcysteine synthetase and glutathione synthetase,
respectively; in 11-d-old seedlings, the corresponding values were 4.5% for
fresh weight, 8.0% for protein content, and 14 and 20% for the enzyme
activities. The highest concentrations of thiols were found for cysteine
(0.27 mM) in the roots, for glutathione (4.4 mM) in the shoots, and for
[gamma]-glutamylcysteine (13 [mu]M) in the scutella of 3-d-old seedlings.
The enzyme activities of roots were localized in subcellular fractions
after sucrose density gradient centrifugation. Nearly half of the
[gamma]-glutamylcysteine synthetase activity was detected in the root
proplastids of 4-d-old seedlings, whereas <10% of the glutathione
synthetase activity was localized in this organelle. Our results
demonstrate the importance of scutella in glutathione synthesis in the
early stage of seedling development. Unlike chloroplasts, root plastids
show only a small proportion of glutathione synthetase activity.
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