Photorespiratory metabolism and immunogold localization of photorespiratory enzymes in leaves of C3 and C 3-C 4 intermediate species of Moricandia.
Photorespiratory metabolism of the C3-C4 intermediate species Moricandia arvensis (L.) DC has been compared with that of the C3 species, Moricandia moricandioides (Boiss.) Heywood. Assays of glycollate oxidase (EC 1.1.3.1), glyoxylate aminotransferases (EC 2.6.1.4, EC 2.6.1.45) and hydroxypyruvate reductase (EC 1.1.1.29) indicate that the capacity for flux through the photorespiratory cycle is similar in both species. Immunogold labelling with monospecific antibodies was used to investigate the cellular locations of ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39), glycollate oxidase, and glycine decarboxylase (EC 2.1.2.10) in leaves of the two species. Ribulose 1,5-bisphosphate carboxylase/oxygenase was confined to the stroma of chloroplasts and glycollate oxidase to the peroxisomes of all photosynthetic cells in leaves of both species. However, whereas glycine decarboxylase was present in the mitochondria of all photosynthetic cells in M. moricandioides, it was only found in the mitochondria of bundle-sheath cells in M. arvensis. We suggest that localized decarboxylation of glycine in the leaves of M. arvensis will lead to improved recapture of photorespired CO2 and hence a lower rate of photorespiration.
AFRC Institute of Plant Science Research, John Innes Institute, Colney Lane, NR4 7UH, Norwich, UK.
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Rawsthorne
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Hylton
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Smith
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Woolhouse