Plant Physiology 96:952-956 (1991)
© 1991 American Society of Plant Biologists
Metabolism and Enzymology
Changes to the Stoichiometry of Glycine Decarboxylase Subunits during Wheat (Triticum aestivum L.) and Pea (Pisum sativum L.) Leaf Development 1
W. John Rogers,
Brian R. Jordan,
Stephen Rawsthorne and
Alyson K. Tobin
Biology Department, School of Biological Sciences, University of Sussex, Falmer, Brighton, Sussex, BN1 9QG, United Kingdom,
Department of Molecular Biology, Horticultural Research International, Worthing Road, Littlehampton, West Sussex, BN17 6LP, United Kingdom,
Cambridge Laboratory, John Innes Centre for Plant Science Research, Colney Lane, Norwich, NR4 7UH, United Kingdom,
Plant Metabolism Research Unit, Department of Cell and Structural Biology, Williamson Building, University of Manchester, Manchester, M13 9PL, United Kingdom
Changes in the levels of the four subunits of the mitochondrial enzyme glycine decarboxylase (EC 2.1.2.10) have been investigated during development in the 8 day old primary leaf of wheat (Triticum aestivum L.). Proteins were extracted from wheat leaf sections between the basal meristem and 8.5 centimeters. The individual glycine decarboxylase subunits were detected by Western blotting, using subunit-specific polyclonal antibodies, and quantified by laser densitometry. P, T, and H subunits showed similar developmental patterns along the leaf. All were below the level of detection up to 1.5 centimeters from the meristem, but then increased over the leaf length examined. In contrast, the increase in the L protein (lipoamide dehydrogenase) was more gradual, and levels in the youngest regions of the leaf were maintained at approximately 14% of those at 8.5 centimeters. In a complementary study, levels of the four subunits in light-grown leaf tissues were compared to those in etiolated leaves from wheat and pea (Pisum sativum L.), using the activity of the mitochondrial marker enzyme fumarase as the basis for comparison. For both wheat and pea, levels of P, T, and H proteins in etiolated tissues were between 25 and 30% of those in lightgrown tissue. However, in etiolated tissues L protein was present at levels of 60 to 70% of that in light-grown tissues. The results indicate that discrete mechanisms may control the synthesis of L, as compared to P, T, and H proteins.
1 Supported by the Agricultural and Food Research Council (grant number PG85/500 to A. K. T.) and by The Royal Society (University Research Fellowship to A. K. T.).
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