Journal of Experimental Botany, Vol. 53, No. 379, pp. 2305-2314,
December 1, 2002
© 2002 Oxford University Press
Utilization of glycine and serine as nitrogen sources in the roots of Zea mays and Chamaegigas intrepidus
Received 4 March 2002; Accepted 3 July 2002
1 Julius-von-Sachs Institut für Biowissenschaften, Lehrstuhl Botanik I, Universität Würzburg, Julius-von-Sachs Platz 2, D-97082 Würzburg, Germany
2 Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, UK
3 To whom correspondence should be addressed. Fax: +44 (0)1865 275074. E-mail: george.ratcliffe{at}plants.ox.ac.uk
Glycine and serine are potential sources of nitrogen for the aquatic resurrection plant Chamaegigas intrepidus Dinter in the rock pools that provide its natural habitat. The pathways by which these amino acids might be utilized were investigated by incubating C. intrepidus roots and maize (Zea mays) root tips with [15N]glycine, [15N]serine and [2-13C]glycine. The metabolic fate of the label was followed using in vivo NMR spectroscopy, and the results were consistent with the involvement of the glycine decarboxylase complex (GDC) and serine hydroxymethyltransferase (SHMT) in the utilization of glycine. In contrast, the labelling patterns provided no evidence for the involvement of serine:glyoxylate aminotransferase in the metabolism of glycine by the root tissues. The key observations were: (i) the release of [15N]ammonium during [15N]-labelling experiments; and (ii) the detection of a characteristic set of serine isotopomers in the [2-13C]glycine experiments. The effects of aminoacetonitrile, amino-oxyacetate, and isonicotinic acid hydrazide, all of which inhibit GDC and SHMT to some extent, and of methionine sulphoximine, which inhibited the reassimilation of the ammonium, supported the conclusion that GDC and SHMT were essential for the metabolism of glycine. C. intrepidus was observed to metabolize serine more readily than the maize root tips and this may be an adaptation to its nitrogen-deficient habitat. Overall, the results support the emerging view that GDC is an essential component of glycine catabolism in non-photosynthetic tissues.
Key words: Glycine decarboxylase, nitrogen nutrition, NMR spectroscopy, non-photosynthetic glycine metabolism.
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