Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1996 Jan;110(1):105–110. doi: 10.1104/pp.110.1.105

The Fungicide Phosphonate Disrupts the Phosphate-Starvation Response in Brassica nigra Seedlings.

C Carswell 1, B R Grant 1, M E Theodorou 1, J Harris 1, J O Niere 1, W C Plaxton 1
PMCID: PMC157699  PMID: 12226174

Abstract

The development of Brassica nigra seedlings over 20 d of growth was disrupted by the fungicide phosphonate (Phi) in a manner inversely correlated with nutritional inorganic phosphate (Pi) levels. The growth of Pi-sufficient (1.25 mM Pi) seedlings was suppressed when 10, but not 5, mM Phi was added to the nutrient medium. In contrast, the fresh weights and root:shoot ratios of Pi-limited (0.15 mM) seedlings were significantly reduced at 1.5 mM Phi, and they progressively declined to about 40% of control values as medium Phi concentration was increased to 10 mM. Intracellular Pi levels generally decreased in Phi-treated seedlings, and Phi accumulated in leaves and roots to levels up to 6- and 16-fold that of Pi in Pi-sufficient and Pi-limited plants, respectively. Extractable activities of the Pi-starvation-inducible enzymes phosphoenolpyruvate phosphatase and inorganic pyrophosphate-dependent phosphofructokinase were unaltered in Pi-sufficient seedlings grown on 5 or 10 mM Phi. However, when Pi-limited seedlings were grown on 1.5 to 10 mM Phi (a) the induction of phosphoenolpyruvate phosphatase and inorganic pyrophosphate-dependent phosphofructokinase activities by Pi limitation was reduced by 40 to 90%, whereas (b) soluble protein concentrations and the activities of the ATP-dependent phosphofructokinase and pyruvate kinase were unaffacted. It is concluded that Phi specifically interrupts processes involved in regulation of the Pi-starvation response in B. nigra.

Full Text

The Full Text of this article is available as a PDF (1.0 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Harold F. M. Inorganic polyphosphates in biology: structure, metabolism, and function. Bacteriol Rev. 1966 Dec;30(4):772–794. doi: 10.1128/br.30.4.772-794.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Penefsky H. S. Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. J Biol Chem. 1977 May 10;252(9):2891–2899. [PubMed] [Google Scholar]
  4. ROBERTSON H. E., BOYER P. D. Orthophosphite as a buffer for biological studies. Arch Biochem Biophys. 1956 Jun;62(2):396–401. doi: 10.1016/0003-9861(56)90137-0. [DOI] [PubMed] [Google Scholar]
  5. Theodorou M. E., Cornel F. A., Duff S. M., Plaxton W. C. Phosphate starvation-inducible synthesis of the alpha-subunit of the pyrophosphate-dependent phosphofructokinase in black mustard suspension cells. J Biol Chem. 1992 Oct 25;267(30):21901–21905. [PubMed] [Google Scholar]
  6. Theodorou M. E., Plaxton W. C. Metabolic Adaptations of Plant Respiration to Nutritional Phosphate Deprivation. Plant Physiol. 1993 Feb;101(2):339–344. doi: 10.1104/pp.101.2.339. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES