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. 1989 May;90(1):151–156. doi: 10.1104/pp.90.1.151

Iron-Stress Induced Redox Activity in Tomato (Lycopersicum esculentum Mill.) Is Localized on the Plasma Membrane 1

Thomas J Buckhout 1,2, Paul F Bell 1,2, Douglas G Luster 1,2,2, Rufus L Chaney 1,2
PMCID: PMC1061690  PMID: 16666726

Abstract

Tomato plants (Lycopersicum esculentum Mill.) were grown for 21-days in a complete hydroponic nutrient solution including Fe3+-ethylenediamine-di(o-hydroxyphenylacetate) and subsequently switched to nutrient solution withholding Fe for 8 days to induce Fe stress. The roots of Fe-stressed plants reduced chelated Fe at rates sevenfold higher than roots of plants grown under Fe-sufficient conditions. The response in intact Fe-deficient roots was localized to root hairs, which developed on secondary roots during the period of Fe stress. Plasma membranes (PM) isolated by aqueous two-phase partitioning from tomato roots grown under Fe stress exhibited a 94% increase in rates of NADH-dependent Fe3+-citrate reduction compared to PM isolated from roots of Fe-sufficient plants. Optimal detection of the reductase activity required the presence of detergent indicating structural latency. In contrast, NADPH-dependent Fe3+-citrate reduction was not significantly different in root PM isolated from Fe-deficient versus Fe-sufficient plants and proceeded at substantially lower rates than NADH-dependent reduction. Mg2+-ATPase activity was increased 22% in PM from roots of Fe-deficient plants compared to PM isolated from roots of Fe-sufficient plants. The results localized the increase in Fe reductase activity in roots grown under Fe stress to the PM.

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Selected References

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

  1. Barrett-Lennard E. G., Marschner H., Römheld V. Mechanism of Short Term Fe Reduction by Roots : Evidence against the Role of Secreted Reductants. Plant Physiol. 1983 Dec;73(4):893–898. doi: 10.1104/pp.73.4.893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bienfait H. F. Regulated redox processes at the plasmalemma of plant root cells and their function in iron uptake. J Bioenerg Biomembr. 1985 Apr;17(2):73–83. doi: 10.1007/BF00744199. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Cakmak I., van de Wetering D. A., Marschner H., Bienfait H. F. Involvement of superoxide radical in extracellular ferric reduction by iron-deficient bean roots. Plant Physiol. 1987 Sep;85(1):310–314. doi: 10.1104/pp.85.1.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chaney R. L., Brown J. C., Tiffin L. O. Obligatory reduction of ferric chelates in iron uptake by soybeans. Plant Physiol. 1972 Aug;50(2):208–213. doi: 10.1104/pp.50.2.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Crane F. L., Sun I. L., Clark M. G., Grebing C., Löw H. Transplasma-membrane redox systems in growth and development. Biochim Biophys Acta. 1985 Aug 1;811(3):233–264. doi: 10.1016/0304-4173(85)90013-8. [DOI] [PubMed] [Google Scholar]
  7. Hodges T. K., Leonard R. T. Purification of a plasma membrane-bound adenosine triphosphatase from plant roots. Methods Enzymol. 1974;32:392–406. doi: 10.1016/0076-6879(74)32039-3. [DOI] [PubMed] [Google Scholar]
  8. Landsberg E. C. Function of Rhizodermal Transfer Cells in the Fe Stress Response Mechanism of Capsicum annuum L. Plant Physiol. 1986 Oct;82(2):511–517. doi: 10.1104/pp.82.2.511. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lutter R., van Zwieten R., Weening R. S., Hamers M. N., Roos D. Cytochrome b, flavins, and ubiquinone-50 in enucleated human neutrophils (polymorphonuclear leukocyte cytoplasts). J Biol Chem. 1984 Aug 10;259(15):9603–9606. [PubMed] [Google Scholar]
  10. Römheld V., Marschner H. Mechanism of iron uptake by peanut plants : I. Fe reduction, chelate splitting, and release of phenolics. Plant Physiol. 1983 Apr;71(4):949–954. doi: 10.1104/pp.71.4.949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Römheld V., Müller C., Marschner H. Localization and capacity of proton pumps in roots of intact sunflower plants. Plant Physiol. 1984 Nov;76(3):603–606. doi: 10.1104/pp.76.3.603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Sijmons P. C., Lanfermeijer F. C., de Boer A. H., Prins H. B., Bienfait H. F. Depolarization of Cell Membrane Potential during Trans-Plasma Membrane Electron Transfer to Extracellular Electron Acceptors in Iron-Deficient Roots of Phaseolus vulgaris L. Plant Physiol. 1984 Dec;76(4):943–946. doi: 10.1104/pp.76.4.943. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sijmons P. C., van den Briel W., Bienfait H. F. Cytosolic NADPH is the electron donor for extracellular fe reduction in iron-deficient bean roots. Plant Physiol. 1984 May;75(1):219–221. doi: 10.1104/pp.75.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tipton C. L., Thowsen J. Fe reduction in cell walls of soybean roots. Plant Physiol. 1985 Oct;79(2):432–435. doi: 10.1104/pp.79.2.432. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. de Vos C. R., Lubberding H. J., Bienfait H. F. Rhizosphere acidification as a response to iron deficiency in bean plants. Plant Physiol. 1986 Jul;81(3):842–846. doi: 10.1104/pp.81.3.842. [DOI] [PMC free article] [PubMed] [Google Scholar]

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