Ammonium can stimulate nitrate and nitrite reductase in the absence of nitrate in Clematis vitalba

  • R. A. Bungard
  • , A. Wingler
  • , J. D. Morton
  • , M. Andrews
  • , M. C. Press
  • , J. D. Scholes

Research output: Contribution to journalArticlepeer-review

Abstract

Nitrogen assimilation was studied in the deciduous, perennial climber Clematis vitalba. When solely supplied with NO3/- in a hydroponic system, growth and N-assimilation characteristics were similar to those reported for a range of other species. When solely supplied with NH4/+, however, nitrate reductase (NR) activity dramatically increased in shoot tissue, and particularly leaf tissue, to up to three times the maximum level achieved in NO3- supplied plants. NO3/- was not detected in plant material that had been solely supplied with NH4/+, there was no NO3/- contamination of the hydroponic system, and the NH4+-induced activity did not occur in tobacco or barley grown under similar conditions. Western Blot analysis revealed that the induction of NR activity, either by NO3/- or NH4/+, was matched by NR and nitrite reductase protein synthesis, but this was not the case for the ammonium assimilation enzyme glutamine synthetase. Exposure of leaf disks to N revealed that NO3/- assimilation was induced in leaves directly by NO3/- and NH4/+ but not glutamine. Our results suggest that the NH4/+-induced potential for NO3/- assimilation occurs when externally sourced NH4/+ is assimilated in the absence of any NO3/- assimilation. These data show that the potential for nitrate assimilation in C. vitalba is induced by a nitrogenous compound in the absence of its substrate and suggest that NO3/- assimilation in C. vitalba may have a significant role beyond the supply of reduced N for growth.

Original languageEnglish
Pages (from-to)859-866
Number of pages8
JournalPlant, Cell and Environment
Volume22
Issue number7
DOIs
Publication statusPublished - 1999
Externally publishedYes

Keywords

  • Ammonium
  • Clematis vitalba
  • Glutamine synthetase
  • Nitrate
  • Nitrate reductase
  • Nitrite reductase
  • Nitrogen
  • PH

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