Hostname: page-component-8448b6f56d-t5pn6 Total loading time: 0 Render date: 2024-04-23T11:35:48.864Z Has data issue: false hasContentIssue false
  • English
  • Français

The mechanism of resistance to aryloxyphenoxypropionate and cyclohexanedione herbicides in a johnsongrass biotype

Published online by Cambridge University Press:  20 January 2017

Kevin W. Bradley ,
Jingrui Wu ,
Kriton K. Hatzios  and
Edward S. Hagood Jr.
Kevin W. Bradley
Affiliation:
Department of Plant Pathology, Physiology, and Weed Science, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061
Jingrui Wu
Affiliation:
Monsanto Company, Gene Mining and Development, 800 North Lindbergh Boulevard, St. Louis, MO 63167
Kriton K. Hatzios
Affiliation:
Department of Plant Pathology, Physiology, and Weed Science, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061
Get access Rights & Permissions [Opens in a new window]

Abstract

Acetyl-coenzyme A carboxylase (ACCase) assays and absorption, translocation, and metabolism experiments were conducted to investigate the mechanism(s) responsible for resistance in a johnsongrass biotype that exhibited low levels of resistance to the cyclohexanedione (CHD) herbicide sethoxydim and the aryloxyphenoxypropionate (APP) herbicides quizalofop-P and fluazifop-P. The rate of [14C]quizalofop-ethyl absorption was significantly higher in the resistant compared to the susceptible biotype 8, 24, and 48 h after treatment (HAT), but by 72 HAT, there was no significant difference in the amount of [14C]quizalofop-ethyl detected in either biotype. Additionally, little or no differences in the translocation of [14C]quizalofop-ethyl were observed in the resistant and susceptible biotypes at any time interval after application. In [14C]quizalofop-ethyl metabolism experiments, similar levels of quizalofop-ethyl and quizalofop metabolites were observed in the resistant and susceptible biotypes 8, 24, 48, and 72 HAT, but slightly higher levels of quizalofop acid were detected in the resistant biotype 48 and 72 HAT. In ACCase assays, the concentrations of quizalofop-P, clethodim, and sethoxydim that inhibited ACCase activity by 50% (I50) were statistically similar in the two biotypes, indicating that the resistant johnsongrass biotype contains an ACCase that is sensitive to the APP and CHD herbicides. In the absence of APP or CHD herbicides, however, the specific activity of ACCase in the resistant biotype was two to three times greater than that of the susceptible biotype. The specific activity of ACCase in the resistant biotype was also significantly greater than that of the susceptible biotype in the presence of all concentrations of quizalofop-P and sethoxydim and in the presence of 0.1, 1, and 10 µM clethodim. These results suggest that resistance to quizalofop-P and sethoxydim is conferred by an overproduction of ACCase in the resistant johnsongrass biotype.

Keywords

Clethodimfluazifop-Pquizalofop-Psethoxydimjohnsongrass, Sorghum halepense (L.) Pers. SORHAAbsorptionACCaseacetyl-CoA carboxylaseenzyme amplificationenzyme overproductionherbicide resistancetranslocation
Type
Research Article
Information
Weed Science , Volume 49 , Issue 4 , August 2001 , pp. 477 - 484
Copyright
Copyright © 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

Bartley, G. E., Maxwell, C. A., Wittenbach, V. A., and Scolnik, P. A. 1997. Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate dioxygenases (Accession No. U89267). Plant Physiol. 113:1465. (Plant Gene Register PGR 97-065)Google Scholar
Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248–254.CrossRefGoogle Scholar
Bradley, K. W., Wu, J., Hagood, E. S. Jr., and Hatzios, K. K. 1999. Investigations on the mechanism of resistance to sethoxydim and quizalofop in a biotype of johnsongrass (Sorghum halepense) from Virginia. Weed Sci. Soc. Am. Abstr. 39:79.Google Scholar
Burton, J. D., Gronwald, J. W., Keith, R. A., Somers, D. A., Gengenbach, B. G., and Wyse, D. A. 1991. Kinetics of inhibition of acetyl coenzyme A carboxylase by sethoxydim and haloxyfop. Pestic. Biochem. Physiol. 39:100–109.CrossRefGoogle Scholar
Caretto, S., Giardina, M. C., Nicolodi, C., and Mariotti, D. 1994. Chlorsulfuron resistance in Daucus carota cell lines and plants: involvement of gene amplification. Theor. Appl. Genet. 88:520–524.CrossRefGoogle ScholarPubMed
Cocker, K. M., Moss, S. R., and Coleman, J.O.D. 1999. Multiple mechanisms of resistance to fenoxaprop-P-ethyl in United Kingdom and other European populations of herbicide-resistant Alopecurus myosuroides (black-grass). Pestic. Biochem. Physiol. 65:169–180.CrossRefGoogle Scholar
Cummins, I., Moss, S., Cole, D. J., and Edwards, R. 1997. Glutathione transferases in herbicide-resistant and herbicide-susceptible black-grass (Alopecurus myosuroides). Pestic. Sci. 51:244–250.3.0.CO;2-2>CrossRefGoogle Scholar
DePrado, J. L., DePrado, R. A., and Shimabukuro, R. H. 1999. The effect of diclofop on membrane potential, ethylene induction, and herbicide phytotoxicity in resistant and susceptible biotypes of grasses. Pestic. Biochem. Physiol. 63:1–14.CrossRefGoogle Scholar
Devine, M. D. 1997. Mechanisms of resistance to acetyl-coenzyme A carboxylase inhibitors: a review. Pestic. Sci. 51:259–264.3.0.CO;2-S>CrossRefGoogle Scholar
Devine, M. D. and Shimabukuro, R. H. 1994. Resistance to acetyl coenzyme A carboxylase inhibiting herbicides. Pages 141–169 In Powles, S. B. and Holtum, J.A.M., eds. Herbicide Resistance: Biology and Biochemistry. Boca Raton, FL.: Lewis.Google Scholar
Dewaele, E., Forlani, G., Degrande, D., Nielsen, E., and Rambour, S. 1997. Biochemical characterization of chlorsulfuron resistance in Cichorium intybus L. var. Witloof. J. Plant Physiol. 151:109–114.CrossRefGoogle Scholar
DiTomaso, J. M. 1994. Evidence against a direct membrane effect in the mechanism of action of graminicides. Weed Sci. 42:302–309.CrossRefGoogle Scholar
Donn, G., Tischer, E., Smith, J. A., and Goodman, H. M. 1984. Herbicide-resistant alfalfa cells: an example of gene amplification in plants. J. Mol. Appl. Genet. 2:621–635.Google ScholarPubMed
Gronwald, J. W. 1991. Lipid biosynthesis inhibitors. Weed Sci. 39:435–449.CrossRefGoogle Scholar
Gronwald, J. W., Eberlein, C. V., Betts, K. J., Baerg, R. J., Ehlke, N. J., and Wyse, D. L. 1992. Mechanism of diclofop resistance in an Italian ryegrass (Lolium multiflorum Lam.) biotype. Pestic. Biochem. Physiol. 44:126–139.CrossRefGoogle Scholar
Hall, L. M., Moss, S. R., and Powles, S. B. 1997. Mechanisms of resistance to aryloxyphenoxypropionate herbicides in two resistant biotypes of Alopecurus myosuroides (blackgrass): herbicide metabolism as a cross-resistance mechanism. Pestic. Biochem. Physiol. 57:87–98.CrossRefGoogle Scholar
Harms, C. T., Armour, S. L., DiMaio, J. J., et al. 1992. Herbicide resistance due to amplification of a mutant acetohydroxyacid synthase gene. Mol. Gen. Genet. 233:427–435.CrossRefGoogle ScholarPubMed
Harwood, J. L. 1988. Fatty acid metabolism. Ann. Rev. Plant Physiol. Plant Mol. Biol. 39:101–138.CrossRefGoogle Scholar
Häusler, R. E., Holtum, J.A.M., and Powles, S. B. 1991. Cross-resistance to herbicides in annual ryegrass (Lolium rigidum). IV. Correlation between membrane effects and resistance to graminicides. Plant Physiol. 97:1035–1043.Google ScholarPubMed
Heap, I. 2000. International survey of herbicide resistant weeds. Online. Internet. Available at www.weedscience.com. Accessed March 23, 2000.Google Scholar
Hidayat, I. and Preston, C. 1997. Enhanced metabolism of fluazifop acid in a biotype of Digitaria sanguinalis resistant to the herbicide fluazifop-P-butyl. Pestic. Biochem. Physiol. 57:137–146.CrossRefGoogle Scholar
Holtum, J.A.M., Matthews, J. M., Häusler, R. E., Liljegren, D. R., and Powles, S. B. 1991. Cross-resistance to herbicides in annual ryegrass (Lolium rigidum). III. On the mechanism of resistance to diclofop-methyl. Plant Physiol. 97:1026–1034.Google ScholarPubMed
Incledon, B. J. and Hall, J. C. 1999. Inhibition of ACCase220 and ACCase240 isozymes from sethoxydim-resistant and -susceptible maize hybrids. J. Agric. Food Chem. 47:299–304.CrossRefGoogle ScholarPubMed
Koeppe, M. K., Anderson, J. J., and Shalaby, L. M. 1990. Metabolism of [14C]quizalofop-ethyl in soybean and cotton plants. J. Agric. Food Chem. 38:1085–1091.CrossRefGoogle Scholar
Konishi, T. and Sasaki, Y. 1994. Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides. Proc. Natl. Acad. Sci. USA 91:3598–3601.CrossRefGoogle ScholarPubMed
Kuk, Y., Wu, J., Derr, J. F., and Hatzios, K. K. 1999. Mechanism of fenoxaprop resistance in an accession of smooth crabgrass (Digitaria ischaemum). Pestic. Biochem. Physiol. 64:112–123.CrossRefGoogle Scholar
Leach, G. E., Devine, M. D., Kirkwood, R. C., and Marshall, G. 1995. Target enzyme-based resistance to acetyl-coenzyme A carboxylase inhibitors in Eleusine indica . Pestic. Biochem. Physiol. 51:129–136.CrossRefGoogle Scholar
Maneechote, C., Holtum, J.A.M., Preston, C., and Powles, S. B. 1994. Resistant acetyl-CoA carboxylase is a mechanism of herbicide resistance in a biotype of Avena sterilis ssp. ludoviciana . Plant Cell Physiol. 35:627–635.CrossRefGoogle Scholar
Maneechote, C., Preston, C., and Powles, S. B. 1997. A diclofop-methyl-resistant Avena sterilis biotype with a herbicide-resistant acetyl-coenzyme A carboxylase and enhanced metabolism of diclofop-methyl. Pestic. Sci. 28:105–114.3.0.CO;2-3>CrossRefGoogle Scholar
Marles, M.A.S., Devine, M. D., and Hall, J. C. 1993a. Herbicide resistance in Setaria viridis conferred by a less sensitive form of acetyl coenzyme A carboxylase. Pestic. Biochem. Physiol. 46:7–14.CrossRefGoogle Scholar
Marles, M.A.S., Devine, M. D., and Hall, J. C. 1993b. Herbicide resistance in green foxtail (Setaria viridis (L.) Beauv.) and johnsongrass (Sorghum halepense (L.) Pers.) biotypes conferred by an insensitive form of acetyl coenzyme-A carboxylase. Weed Sci. Soc. Am. Abstr. 33:62.Google Scholar
Menendez, J. and DePrado, R. 1996. Diclofop-methyl cross-resistance in a chlortoluron resistant biotype of Alopecurus myosuroides . Pestic. Biochem. Physiol. 56:123–133.CrossRefGoogle Scholar
Odell, J. T., Caimi, P. G., Yadav, N. S., and Mauvais, C. J. 1990. Comparison of increased expression of wild-type and herbicide-resistant acetolactate synthase genes in transgenic plants, and indication of posttranscriptional limitation on enzyme activity. Plant Physiol. 94:1647–1654.CrossRefGoogle ScholarPubMed
Parker, W. B., Somers, D. A., Wyse, D. L., Keith, R. A., Burton, J. D., Gronwald, J. W., and Gengenbach, B. G. 1990. Selection and characterization of sethoxydim-tolerant maize tissue cultures. Plant Physiol. 92:1220–1225.CrossRefGoogle ScholarPubMed
Ruizzo, M. A. and Gorski, S. F. 1988. Inhibition of chloroplast-mediated reactions by quizalofop herbicide. Weed Sci. 36:713–718.CrossRefGoogle Scholar
Seefeldt, S. S., Fuerst, E. P., Gealy, D. R., Shukla, A., Irzyk, G. P., and Devine, M. D. 1996. Mechanisms of resistance to diclofop of two wild oat (Avena fatua) biotypes from the Willamette Valley of Oregon. Weed Sci. 44:776–781.CrossRefGoogle Scholar
Shukla, A., Dupont, S., and Devine, M. D. 1997a. Resistance to ACCase-inhibitor herbicides in wild oat: evidence for target site-based resistance in two biotypes from Canada. Pestic. Biochem. Physiol. 57:147–155.CrossRefGoogle Scholar
Shukla, A., Leach, G. E., and Devine, M. D. 1997b. High-level resistance to sethoxydim conferred by an alteration in the target enzyme, acetyl-CoA carboxylase, in Setaria faberi and Setaria viridis . Plant Physiol. Biochem. 35:803–807.Google Scholar
Smeda, R. J., Snipes, C. E., and Barrentine, W. L. 1997. Identification of graminicide-resistant johnsongrass (Sorghum halepense). Weed Sci. 45:132–137.CrossRefGoogle Scholar
Stoltenberg, D. E., Gronwald, J. W., Wyse, D. L., Burton, J. D., Somers, D. A., and Gengenbach, B. G. 1989. Effect of sethoxydim and haloxyfop on acetyl-coenzyme A carboxylase activity in Festuca species. Weed Sci. 37:512–515.CrossRefGoogle Scholar
Stoltenberg, D. E. and Wiederholt, R. J. 1995. Giant foxtail (Setaria faberi) resistance to aryloxyphenoxypropionate and cyclohexanedione herbicides. Weed Sci. 45:527–535.CrossRefGoogle Scholar
Tal, A., Zarka, S., and Rubin, B. 1996. Fenoxaprop-P resistance in Phalaris minor conferred by an insensitive acetyl-coenzyme A carboxylase. Pestic. Biochem. Physiol. 56:134–140.CrossRefGoogle Scholar
Tardif, F. J., Holtum, J.A.M., and Powles, S. B. 1993. Occurrence of a herbicide-resistant acetyl-coenzyme A carboxylase mutant in annual ryegrass (Lolium rigidum) selected by sethoxydim. Planta 190:176–181.CrossRefGoogle Scholar
Tardif, F. J. and Powles, S. B. 1994. Herbicide multiple-resistance in a Lolium rigidum biotype is endowed by multiple mechanisms: isolation of a subset with resistant acetyl-CoA carboxylase. Physiol. Plant. 91:488–494.CrossRefGoogle Scholar
VanGessel, M. J., Johnson, Q., and Isaacs, M. 1997. Response of sethoxydim-resistant corn (Zea mays) hybrids to postemergence graminicides. Weed Technol. 11:598–601.CrossRefGoogle Scholar
Yu-Yau, J. S., Hepburn, A. G., and Widholm, J. M. 1992. Glyphosate selected amplification of the 5-enolpyruvylshikimate-3-phosphate synthase gene in cultured carrot cells. Mol. Gen. Genet. 232:377–382.Google Scholar