Hostname: page-component-78c5997874-t5tsf Total loading time: 0 Render date: 2024-11-16T09:24:21.121Z Has data issue: false hasContentIssue false
  • English
  • Français

ALS gene proline (197) mutations confer ALS herbicide resistance in eight separated wild radish (Raphanus raphanistrum) populations

Published online by Cambridge University Press:  20 January 2017

Qin Yu ,
Xiao Qi Zhang ,
Abul Hashem ,
Michael J. Walsh  and
Stephen B. Powles
Qin Yu
Affiliation:
Western Australian Herbicide Resistance Initiative, School of Plant Biology, University of Western Australia, Crawley, WA 6009, Australia
Xiao Qi Zhang
Affiliation:
Western Australian Herbicide Resistance Initiative, School of Plant Biology, University of Western Australia, Crawley, WA 6009, Australia
Abul Hashem
Affiliation:
Department of Agriculture, Centre for Cropping Systems, Northam, WA 6401
Michael J. Walsh
Affiliation:
Western Australian Herbicide Resistance Initiative, School of Plant Biology, University of Western Australia, Crawley, WA 6009, Australia
Get access Rights & Permissions [Opens in a new window]

Abstract

The biochemical and molecular basis of resistance to acetolactate synthase (ALS)–inhibiting herbicides was investigated in eight resistant (R) and three susceptible (S) wild radish populations. In vitro enzyme assays revealed an ALS herbicide–resistant ALS enzyme in all R populations. ALS enzyme extracted from the shoots of all eight R populations was highly resistant to the ALS-inhibiting sulfonylurea herbicide chlorsulfuron (20- to 160-fold) and the triazolopyrimidine herbicide metosulam (10- to 46-fold) and moderately resistant to metsulfuron (three to eightfold). There was little or no cross-resistance to the imidazolinone herbicides imazapyr and imazethapyr. The ALS gene fragment covering potential mutation sites in these populations was amplified, sequenced, and compared. All eight R populations had point mutations in the codon for the proline residue in Domain A. However, the point mutations varied and encoded four different amino acid substitutions: histidine, threonine, alanine, and serine. No nucleotide difference in the DNA sequence of Domains C and D resulting in amino acid substitutions was observed between the R and S populations examined. In addition, a three- to fivefold higher ALS-specific activity was consistently observed in all R populations compared with S populations, whereas Northern blot analysis detected a similar level of ALS mRNA, suggesting a possible translational–posttranslational regulation of the enzyme. It is concluded that selection pressure from chlorsulfuron on eight separate wild radish populations has resulted in target site mutation at the same proline residue in the ALS gene. Higher ALS activity also may play a role in the resistance level.

Keywords

Chlorsulfuronflumetsulamimazapyrimazethapyrmetosulammetsulfuronwild radish, Raphanus raphanistrum L. RAPRAAcetolactate synthasetarget site
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 51 , Issue 6 , December 2003 , pp. 831 - 838
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

Adkins, S. W., Wills, D., Boersma, M., Walker, S. R., Robinson, G., McLeod, R. J., and Einam, J. P. 1997. Weed resistance to chlorsulfuron and atrazine from the north-east grain region of Australia. Weed Res 37:343–349.CrossRefGoogle Scholar
Bernasconi, P., Woodworth, A. R., Rosin, B. A., Subramanian, M. V., and Siehl, D. L. 1995. A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. J. Biol. Chem 270:17381–17385.Google Scholar
Boutsalis, P., Karotam, J., and Powles, S. B. 1999. Molecular basis of resistance to acetolactate synthase-inhibiting herbicides in Sisymbrium orientale and Brassica tournefortii . Pestic. Sci 55:507–516.Google Scholar
Boutsalis, P. and Powles, S. B. 1995a. Resistance of dicot weeds to acetolactate synthase (ALS)-inhibiting herbicides in Australia. Weed Res 35:149–155.CrossRefGoogle Scholar
Boutsalis, P. and Powles, S. B. 1995b. Inheritance and mechanism of resistance to herbicides inhibiting acetolactate systhase in Sonchus oleraceus L. Theor. Appl. Genet 91:242–247.Google Scholar
Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein binding. Anal. Biochem 72:248–254.Google Scholar
Christopher, J. T., Powles, S. B., and Holtum, J. A. M. 1992. Resistance to acetolactate synthase–inhibiting herbicides in annual ryegrass (Lolium rigidum) involves at least two mechanisms. Plant Physiol 100:1909–1913.CrossRefGoogle ScholarPubMed
Christopher, J. T., Powles, S. B., Liljegren, D. R., and Holtum, J. A. M. 1991. Cross-resistance to herbicides in annual ryegrass (Lolium rigidum). II. Chlorsulfuron resistance involves a wheat-like detoxification system. Plant Physiol 100:1036–1043.Google Scholar
Cotterman, J. C. and Saari, L. L. 1992. Rapid metabolic inactivation is the basis for cross-resistance to chlorsulfuron in diclofop-methyl-resistant rigid ryegrass (Lolium rigidum) biotype SR4/84. Pestic. Biochem. Physiol 43:182–192.Google Scholar
Devine, M. D. and Eberlein, C. V. 1997. Physiological, biochemical and molecular aspects of herbicide resistance based on altered target sites. Pages 159–185 in Michael Roe, R., Burton, J. D., and Kuhr, R. J. eds. Herbicide Activity: Toxicology, Biochemistry and Molecular Biology. Amsterdam, The Netherlands: IOS.Google Scholar
Dewaele, E., Forlani, G., Degrande, D., Nielsen, E., and Rambour, S. 1996. Biochemical characterization of chlorsulfuron resistance in Cichorium intybus L. var. Witloof. J. Plant Physiol 151:109–114.CrossRefGoogle Scholar
Doyle, J. J. and Doyle, J. L. 1990. Isolation of plant DNA from fresh tissue. Focus 12:13–15.Google Scholar
Eberlein, C. V., Guttieri, M. J., Berger, P. H., Fellman, J. K., Mallory-Smith, C. A., Thill, D. C., Baerg, R. J., and Belknap, W. R. 1999. Physiological consequence of mutation for ALS-inhibitor resistance. Weed Sci 47:383–392.Google Scholar
Fisher, A. J., Bayer, D. E., Carriere, M. D., Ateh, C. M., and Yim, K. O. 2000. Mechanisms of resistance to bispyribac-sodium in an Echnochloa phyllopogon accession. Pestic. Biochem. Physiol 68:156–165.CrossRefGoogle Scholar
Forlani, G., Nielseren, F., Landi, P., and Tuberosa, R. 1991. Chlorsulfuron tolerance and acetolactate synthase activity in corn (Zea mays L.) inbred lines. Weed Sci 39:553–557.Google Scholar
Guttieri, M. J., Eberlein, C. V., Mallory-Smith, C. A., Thill, D. C., and Hoffman, D. L. 1992. DNA sequence variation in Domain A of the acetolactate synthase genes of herbicide-resistant and -susceptible weed biotypes. Weed Sci 40:670–676.Google Scholar
Guttieri, M. J., Eberlein, C. V., and Thill, D. C. 1995. Diverse mutations in the acetolactate synthase gene confer chlorsulfuoron resistance in kochia (Kochia scoparia) biotypes. Weed Sci 43:175–178.Google Scholar
Hashem, A., Bowran, D., Piper, T., and Dhammu, H. 2001. Resistance of wild radish (Raphanus raphanistrum) to acetolactate synthase-inhibiting herbicides in the Western Australian wheat belt. Weed Technol 15:68–74.CrossRefGoogle Scholar
Hattori, J., Brown, D., Mourad, G., Labbé, H., Ouellet, T., Sunohara, G., Rutledge, R., King, J., and Miki, B. 1995. An acetohydroxyacid synthase mutant reveals a single site involved in multiple herbicide resistance. Mol. Gen. Genet 246:419–425.Google Scholar
Haughn, G. W. and Somerville, C. 1986. Sulfonylurea-resistant mutants of Arabidopsis thaliana . Mol. Gen. Genet 204:430–434.Google Scholar
Heap, I. 2002. International Survey of Herbicide Resistant Weeds. www.weedscience.com.Google Scholar
Llewellyn, R. S. and Powles, S. B. 2001. High levels of herbicide resistance in rigid ryegrass (Lolium rigidum) in the wheat belt of Western Australia. Weed Technol 15:242–248.CrossRefGoogle Scholar
Menendez, J. M., De Prado, R., and Devine, M. D. 1997. Chlorsulfuron cross-resistance in a chlorotoluron-resistant biotype of Alopecurus myosuroides . Page 319 in Proc. Brighton Crop. Prot. Conf.—Weeds. Farnham, UK: The British Crop Protection Council.Google Scholar
Mourad, G. and King, J. 1992. Effect of four classes of herbicides on growth and acetolactase-synthase activity in several variants of Arabidopsis thaliana . Planta 188:491–497.Google 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.Google Scholar
Patzoldt, W. L. and Tranel, P. L. 2002. Molecular analysis of cloransulam resistance in a population of giant ragweed. Weed Sci 50:299–305.Google Scholar
Preston, C. and Mallory-Smith, C. A. 2001. Biochemical mechanisms, inheritance, and molecular genetics of herbicide resistance in weeds. Pages 23–60 in Powles, S. B. and Shaner, D. L. eds. Herbicide Resistance and World Grains. Boca Raton, FL: CRC.CrossRefGoogle Scholar
Rathinasabapathi, B., Williams, D., and King, J. 1990. Altered feedback sensitivity to valine, leucine and isoleucine of acetolactate synthase from herbicide-resistant variants of Datura innoxia . Plant Sci 67:1–6.Google Scholar
Ray, T. B. 1984. Site of action of chlorsulfuron—inhibition of valine and isoleucine biosynthesis in plants. Plant Physiol 75:827–831.CrossRefGoogle ScholarPubMed
Saari, L. L., Cotterman, J. C., and Thill, D. C. 1994. Resistance to acetolactate synthase inhibiting herbicide. Pages 83–139 in Powles, S. B. and Holtum, J.A.M. eds. Herbicide Resistance in Plants, Biology and Biochemistry. Boca Raton, FL: Lewis.Google Scholar
Saari, L. L. and Mauvais, C. J. 1996. Sulfonylurea herbicide-resistant crops. Pages 127–142 in Duke, S. O. ed. Herbicide Resistant Crops. Boca Raton, FL: Lewis.Google Scholar
Santel, H. J., Bowden, B. A., Sorensen, V. M., and Mueller, K. H. 1999. Flucarbazone-sodium—a new herbicide for the control of wild oat and green foxtail in wheat. Page 23 in Proc. Brighton Crop Prot. Conf.—Weeds. Farnham, UK: The British Crop Protection Council.Google Scholar
Subramanian, M. V., Lonvy-Gallant, V., Dias, J. M., and Mireles, L. C. 1991. Acetolactate synthase inhibiting herbicides bind to the regulatory site. Plant Physiol 96:310–313.CrossRefGoogle Scholar
Tan, M. K. and Medd, R. W. 2002. Characterisation of the acetolactate synthase (ALS) gene of Raphanus raphanistrum L. and the molecular assay of mutations associated with herbicide resistance. Plant Sci 163:195–205.CrossRefGoogle Scholar
Tranel, P. J. and Wright, T. R. 2003. Resistance of weeds to ALS inhibiting herbicides: what have we learned. Weed Sci 50:700–712.Google Scholar
Uchino, A. and Watanabe, H. 2002. Mutations in the acetolactate synthase genes of sulfonylurea-resistant biotypes of Lindernia spp. Weed Biol. Manag 2:104–109.Google Scholar
Veldhuis, L. J., Hall, L. M., O'Donovan, J. T., Dyer, W., and Hall, J. C. 2000. Metabolism-based resistance of a wild mustard (Sinapis arvensis L.) biotype to ethametsulfuron-methyl. J. Agric. Food Chem 48:2986–2990.Google Scholar
Venugopalan, C. and Kapoor, H. C. 1997. Single step isolation of plant RNA. Phytochemistry 46:1303–1305.Google Scholar
Walsh, M. J., Duane, R. D., and Powles, S. B. 2001. High frequency of chlorsulfuron-resistant wild radish (Raphanus raphanistrum) populations across the Western Australian wheat belt. Weed Technol 15:199–203.Google Scholar
Woodworth, A. R., Rosen, R. A., and Bernasconi, P. 1996. Broad range resistance to herbicides targeting acetolactate synthase (ALS) in a field isolate of Amaranthus sp. is conferred by a Trp to Leu mutation in the ALS gene (Accession No. U55852) (PGR96-051). Plant Physiol 111:1353.Google Scholar
Wright, T. R., Bascomb, N. F., Sturner, S. F., and Penner, D. 1998. Biochemical mechanism and molecular basis for ALS-inhibiting herbicide resistance in sugarbeet (Beta vulgaris) somatic cell selections. Weed Sci 46:13–23.CrossRefGoogle Scholar