Hostname: page-component-78c5997874-g7gxr Total loading time: 0 Render date: 2024-11-13T04:06:58.316Z Has data issue: false hasContentIssue false
  • English
  • Français

Revisiting auxin transport inhibition as a mode of action for herbicides

Published online by Cambridge University Press:  12 June 2017

Mani V. Subramanian ,
Sandra A. Brunn ,
Paul Bernasconi ,
Bhavesh C. Patel  and
Jeff D. Reagan
Mani V. Subramanian*
Affiliation:
Novartis Crop Protection, Research Division, 975 California Avenue, Palo Alto, CA 94304
Sandra A. Brunn
Affiliation:
Novartis Crop Protection, Research Division, Palo Alto, CA 94304
Paul Bernasconi
Affiliation:
Novartis Crop Protection, Research Division, Palo Alto, CA 94304
Bhavesh C. Patel
Affiliation:
Novartis Crop Protection, Research Division, Palo Alto, CA 94304
Jeff D. Reagan
Affiliation:
Novartis Crop Protection, Research Division, Palo Alto, CA 94304
*
mani.subramanian@cp.novartis.com.
Get access Rights & Permissions [Opens in a new window]

Abstract

SCB-1, a semicarbazone, is a phytotoxin with both preemergence and postemergence activity against broadleaves and grasses. It effectively displaced [3H]naptalam bound to a solubilized plasma membrane fraction, with the concentration required for 50% dissociation being 3.5 nM. The intrinsic dissociation constant (Kd) for binding of [3H]naptalam to zucchini plasma membranes was estimated to be 9.7 nM. Binding of [3H]naptalam to the solubilized protein fraction from the plasma membrane was rapid, time dependent, saturable, and reversible. The Kd for binding was estimated at 4 nM. Based on the maximum binding of [3H]naptalam, concentration of the binding protein was calculated to be 23.6 and 10.8 pmol mg−1 protein in the plasma membrane and solubilized fraction, respectively. SCB-1 also blocked the efflux of [14C]IAA, resulting in more than 800% accumulation of radiolabel in zucchini squash hypocotyl segments at 5 μM. This accumulation was quenched by excess cold IAA and 2,4-D. Collectively, these results suggest that SCB-1 is a potent inhibitor of auxin efflux and that it competes with naptalam for binding to the plasma membrane protein.

Keywords

Naptalam, 2-[(1-naphthalenylamino)carbonyl]benzoic acidSCB-1IAA2,4-DMode of actionauxin transportauxin transport proteinefflux carrier
Type
Symposium
Information
Weed Science , Volume 45 , Issue 5 , October 1997 , pp. 621 - 627
Copyright
Copyright © 1997 by the Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Literature Cited

Ahrens, W. H., ed. 1994. Herbicide Handbook. 7th ed. Champaign, IL: Weed Science Society of America, pp. 214–215.Google Scholar
Anderson, R. J., Leippe, M. L., Bowe, S., King, D. L., Lamoreaux, R. J., and Hess, F. D. 1997. SAN 835H: a new corn herbicide representing a novel chemical class. WSSA Abstr. 37: 15.Google Scholar
Astle, M. C. and Rubery, P. H. 1986. Effects of calmodulin antagonists on transmembrane auxin transport in Cucurbita pepo hypocotyl segments. Plant Sci. 43: 165–172.Google Scholar
Bernasconi, P. 1996. Effect of synthetic and natural protein tyrosine kinase inhibitors on auxin efflux in zucchini (Cucurbita pepo L.) hypocotyls. Physiol. Plant 96: 205–210.CrossRefGoogle Scholar
Bernasconi, P., Patel, B. C., Reagan, J. D., and Subramanian, M. V. 1996. The N-1-naphthylphthalamic acid-binding protein is an integral membrane protein. Plant Physiol. 111: 427–432.CrossRefGoogle ScholarPubMed
Brunn, S., Subramanian, M., Haworth, P., and Schaefer, K. 1997. The mode of action of SAN 835H: inhibition of auxin transport. WSSA Abstr. 37: 70.Google Scholar
Brunn, S., Subramanian, M. V., Walters, E. W., Patel, B. C., and Reagan, J. D. 1994. Biochemical characterization of auxin transport protein using phytotropins. in Hedin, P. A., ed. Bioregulators for Crop Protection and Pest Control. American Chemical Society Symposium Series 557. Washington, DC: American Chemical Society, pp. 203–211.Google Scholar
Dahmer, M. K., Housley, P. R., and Pratt, W. B. 1984. Effects of molybdate and endogenous inhibitors on steroid receptor inactivation, transformation, and translocation. Annu. Rev. Physiol. 46: 67–81.Google Scholar
Guilfoyle, T. J. 1987. Auxin-regulated gene expression in higher plants. CRC Crit. Rev. Plant Sci. 4: 247–276.CrossRefGoogle Scholar
Hoffman, O. L. and Smith, A. E. 1949. A new group of plant growth regulators. Science 109: 588.Google Scholar
Jacobs, M. and Gilbert, S. E. 1983. Basal localization of the presumptive auxin transport carrier in pea stem cells. Science 220: 1297–1300.Google Scholar
Katekar, G. K. and Geissler, A. E. 1977. Auxin transport inhibitots III: chemical requirements of a class of auxin transport inhibitors. Plant Physiol. 60: 826–829.Google Scholar
Katekar, G. K. and Geissler, A. E. 1989. The distribution of the receptor for 1-N-1-naphthylphthalamic acid in different tissues in maize. Physiol. Plant. 76: 183–186.Google Scholar
Lembi, C. A., Morre, D. J., St-Thomson, K., and Hertel, R. 1971. N-1-naphthylphthalamic acid binding activity of a plasma membrane-rich fraction from maize colcoptiles. Planta 76: 183–186.Google Scholar
Lomax, T. L., Mehlhorn, R. J., and Briggs, W. R. 1985. Active auxin uptake by zucchini membrane vesicles: quantitation using ESR volume and pH determinations. Proc. Natl. Acad. Sci. USA 82: 6541–6545.Google Scholar
Lomax, T. L., Muday, G. K., and Rubery, P. H. 1995. Auxin transport. Pages in Davis, P. J., ed. Plant Hormones, Physiology, Biochemistry and Molecular Biology. Boston: Academic Press, pp. 509–530.Google Scholar
Muday, G. K., Brunn, S. A., Hawarth, P., and Subramanian, M. V. 1993. Evidence for a single naphthylphthalamic acid binding site on the zucchini plasma membrane. Plant Physiol. 103: 449–456.Google Scholar
Munson, P. J. and Rodbard, D. 1980. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107: 220–239.Google Scholar
Rubery, P. H. 1987. Auxin transport. in Davis, P. J., ed. Plant Hormones and Their Role in Plant Growth and Development. Hingham, MA: Martinus Nighoff, pp. 341–362.Google Scholar
Rubery, P. H. and Sheldrake, A. R. 1974. Carrier-mediated auxin transport. Planta 118: 101–121.CrossRefGoogle ScholarPubMed
Sherman, M. R. and Stevens, J. 1984. Structure of mammalian steroid receptors: evolving concepts and methodological developments. Annu. Rev. Physiol. 46: 83–105.Google Scholar
Siehl, D. L., Bengtson, A. S., Brockman, J. P., Butler, J. H., Kraatz, G. W., Lamoreaux, R. J., and Subramanian, M. V. 1996. Patterns of cross-tolerance to herbicides inhibiting acetohydroxyacid synthase in commercial corn hybrids designed for tolerance to imidazolinones. Crop Sci. 36: 274–278.Google Scholar
Sussman, M. R. and Gardner, G. 1980. Solubilization of the receptor for N-1-naphthylphthalamic acid. Plant Physiol. 66: 1074–1078.Google Scholar
Sussman, M. R. and Goldsmith, M.H.M. 1981. The mechanism of auxin uptake and action of N-1-naphthylphthalamic acid in corn coleoptiles. Planta 151: 15–25.Google Scholar
Widell, S. and Larsson, C. 1981. Separation of presumptive plasma membranes from mitochondria by partition in an aqueous polymer two phase system. Plant Physiol. 51: 368–374.Google Scholar
Wilkinson, S. and Morris, D. A. 1994. Targeting of auxin carriers to the plasma membrane: effects of monensin on transmembrane auxin transport in Cucurbita pepo L. tissue. Planta 193: 194–202.Google Scholar