Abstract
Maize (Zea mays L.) grown on low (0.8 mM) NO -3 , as well as untransformed and transformed Nicotiana plumbaginifolia constitutively expressing nitrate reductase (NR), was used to study the effects of NO -3 on the NR activation state. The NR activation state was determined from the relationship of total activity extracted in the presence of ethylenediaminetetracetic acid to that extracted in the presence of Mg2+. Light activation was observed in both maize and tobacco leaves. In the tobacco lines, NO -3 did not influence the NR activation state. In excised maize leaves, no correlation was found between the foliar NO -3 content and the NR activation state. Similarly, the NR activation state did not respond to NO -3 . Since the NR activation state determined from the degree of Mg2+-induced inhibition of NR activity is considered to reflect the phosphorylation state of the NR protein, the protein phosphatase inhibitor microcystin LR was used to test the importance of protein phosphorylation in the NO -3 -induced changes in NR activity. In-vivo inhibition of endogenous protein phosphatase activity by microcystin-LR decreased the level of NR activation in the light. This occurred to the same extent in the presence or absence of exogenous NO -3 . We conclude that NO -3 does not effect the NR activation state, as modulated by protein phosphorylation in either tobacco (a C3 species) or maize (a C4 species). The short-term regulation of NR therefore differs from the NO -3 -mediated responses observed for phosphoenolpyruvate carboxylase and sucrose phosphate synthase.
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Abbreviations
- Chl:
-
chlorophyll
- MC:
-
microcystin-LR
- PEP-Case:
-
phosphoenolpyruvate carboxylase
- SPS:
-
sucrose-phosphate synthase
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We are indebted to Madeleine Provot and Nathalie Hayes for excellent technical assistance. This work was funded by EEC Biotechnology Contract No. BI02 CT93 0400, project of technical priority, Network D — Nitrogen Utilisation and Efficiency.
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Ferrario, S., Valadier, MH. & Foyer, C.H. Short-term modulation of nitrate reductase activity by exogenous nitrate in Nicotiana plumbaginifolia and Zea mays leaves. Planta 199, 366–371 (1996). https://doi.org/10.1007/BF00195728
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DOI: https://doi.org/10.1007/BF00195728