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Up-regulation and localization of asparagine synthetase in tomato [Lycopersicon esculentum] leaves infected by the bacterial pathogen Pseudomonas syringae

Nitrogen metabolism is one aspect of basic metabolism, which is still quite unknown in the field of plant-pathogen interactions. Evidence derived from previous studies conducted in our laboratory strongly suggests that during microbial pathogenesis an important nitrogen mobilization process takes pl...

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Bibliographic Details
Published in:Plant and cell physiology 2004-06, Vol.45 (6), p.770-780
Main Authors: Olea, F. (Universidad de Malaga (Spain)), Perez-Garcia, A, Canton, F.R, Rivera, M.E, Canas, R, Avila, C, Cazorla, F.M, Canovas, F.M, de Vicente, A
Format: Article
Language:English
Subjects:
GS1
GS2
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Summary:Nitrogen metabolism is one aspect of basic metabolism, which is still quite unknown in the field of plant-pathogen interactions. Evidence derived from previous studies conducted in our laboratory strongly suggests that during microbial pathogenesis an important nitrogen mobilization process takes place in diseased tissues. Here we describe the expression pattern of asparagine synthetase (AS; EC 6.3.5.4) in tomato leaves infected by the bacterial pathogen Pseudomonas syringae pv. tomato. Using an homologous AS cDNA probe isolated by RT-PCR from infected leaves, we have observed a high level induction of AS expression during the course of infection. Concomitantly, a single AS polypeptide also accumulated in response to bacterial infection. Furthermore, immunohistochemical analysis of AS in infected leaves revealed a strong immunostaining in phloem cells of the main vascular bundles and in secondary veins of the leaf blade. These data correlate with those previously reported for expression of a cytosolic isoform of glutamine synthetase (GS1) also induced during development of the infectious process. Taken together, our results suggest the existence of a GS1/AS pathway representing a metabolic route for transferring ammonium released from protein catabolism into asparagine, an amino acid that may have a major role in nitrogen mobilization from diseased tissues.
ISSN:0032-0781
1471-9053
DOI:10.1093/pcp/pch092