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. 1974 Oct;71(10):4232–4236. doi: 10.1073/pnas.71.10.4232

The Toxin-Binding Protein of Sugarcane, Its Role in the Plant and in Disease Development

Gary A Strobel 1
PMCID: PMC434365  PMID: 16592191

Abstract

The toxin-binding protein of sugarcane susceptible to eyespot disease also possesses raffinose-binding activity. The Km's for binding are: helminthosporoside (toxin) 6.8 × 10-5 M, raffinose 2.5 × 10-5 M, and melibiose 2.6 × 10-5 M. Evidence obtained by administering [14C]raffinose to sugarcane protoplasts suggests that this protein participates in α-galactoside transport. Cells from a resistant clone of sugarcane do not possess an active-binding protein, and likewise, do not actively take up raffinose. Interestingly, the K+, Mg++ ATPase (ATP phosphohydrolase, EC 3.6.1.3.) on the plasma membrane of the susceptible sugarcane is 30% activated by the toxin at 3 mM. In addition, toxin-treated tissue slices show a rapid uptake of 86Rb+-K+ which is in agreement with the toxin activation of the membrane K+, Mg++ ATPase. Since the ATPase does not directly interact with the toxin, the activation effect occurs by means of the toxin-binding protein. Membrane proteins may be influenced by the toxin-binding protein acting by one of several different mechanisms.

Keywords: membranes, helminthosporoside, membrane protein interactions

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Selected References

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

  1. Glasziou K. T. Accumulation and Transformation of Sugars in Sugar Cane Stalks. Plant Physiol. 1960 Nov;35(6):895–901. doi: 10.1104/pp.35.6.895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Hodges T. K., Leonard R. T., Bracker C. E., Keenan T. W. Purification of an ion-stimulated adenosine triphosphatase from plant roots: association with plasma membranes. Proc Natl Acad Sci U S A. 1972 Nov;69(11):3307–3311. doi: 10.1073/pnas.69.11.3307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  4. Leonard R. T., Hodges T. K. Characterization of Plasma Membrane-associated Adenosine Triphosphase Activity of Oat Roots. Plant Physiol. 1973 Jul;52(1):6–12. doi: 10.1104/pp.52.1.6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Läuchli A., Epstein E. Transport of potassium and rubidium in plant roots: the significance of calcium. Plant Physiol. 1970 May;45(5):639–641. doi: 10.1104/pp.45.5.639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Maretzki A., Thom M. Membrane transport of sugars in cell suspensions of sugarcane: I. Evidence for sites and specificity. Plant Physiol. 1972 Feb;49(2):177–182. doi: 10.1104/pp.49.2.177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Moreno A., Cardini C. E. A raffinose-sucrose transgalactosidase from wheat germ. Plant Physiol. 1966 May;41(5):909–910. doi: 10.1104/pp.41.5.909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Steiner G. W., Strobel G. A. Helminthosporoside, a host-specific toxin from Helminthosporium sacchari. J Biol Chem. 1971 Jul 10;246(13):4350–4357. [PubMed] [Google Scholar]
  9. Strobel G. A. Biochemical basis of the resistance of sugarcane to eyespot disease. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1693–1696. doi: 10.1073/pnas.70.6.1693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Strobel G. A., Hess W. M. Evidence for the presence of the toxin-binding protein on the plasma membrane of sugarcane cells. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1413–1417. doi: 10.1073/pnas.71.4.1413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Strobel G. A. The helminthosporoside-binding protein of sugarcane. Its properties and relationship to susceptibility to the eye spot disease. J Biol Chem. 1973 Feb 25;248(4):1321–1328. [PubMed] [Google Scholar]
  12. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]

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