Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-19T04:16:50.682Z Has data issue: false hasContentIssue false
  • English
  • Français

Prevalence of a Novel Resistance Mechanism to PPO-Inhibiting Herbicides in Waterhemp (Amaranthus tuberculatus)

Published online by Cambridge University Press:  20 January 2017

Ryan M. Lee ,
Aaron G. Hager  and
Patrick J. Tranel
Ryan M. Lee
Affiliation:
Department of Crop Sciences, University of Illinois, 1201 West Gregory Drive, Urbana, IL 61801
Aaron G. Hager
Affiliation:
Department of Crop Sciences, University of Illinois, 1201 West Gregory Drive, Urbana, IL 61801
Patrick J. Tranel*
Affiliation:
Department of Crop Sciences, University of Illinois, 1201 West Gregory Drive, Urbana, IL 61801
*
Corresponding author's E-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

Resistance to protoporphyrinogen oxidase (PPO)-inhibiting herbicides in waterhemp has been shown previously to be the result of a unique mechanism. Specifically, a three–base-pair (3-bp) deletion in the PPX2L gene, a gene encoding both plastid- and mitochondria-targeted PPO enzymes, confers herbicide resistance in this species. Furthermore, when this unique mechanism was initially characterized it was presumed that waterhemp contained three PPX genes, PPX1, PPX2S, and PPX2L, and that the resistant biotypes were missing PPX2S. Here, allele testing and examination of genetic sequence data demonstrate that there are likely only two PPX genes in waterhemp, PPX1 and PPX2L. Next, to determine the prevalence of this mechanism of resistance in Illinois waterhemp, we developed an allele-specific polymerase chain reaction (PCR) marker that amplifies only the 3-bp deletion allele, ΔG210, of PPX2L. By utilizing this marker, we show that the ΔG210 PPX2L allele correlated with whole-plant resistance to PPO inhibitors in each of four other waterhemp populations evaluated from Illinois.

Keywords

Common waterhemp, Amaranthus tuberculatus (Moq.) Sauer var. rudis (Sauer) Costea & Tardif AMATUtall waterhemp, Amaranthus tuberculatus (Moq.) Sauer var. tuberculatus (Sauer) Costea & Tardif AMATU.Herbicide resistanceprotoporphyrinogen oxidaseprotoxmolecular marker
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 56 , Issue 3 , June 2008 , pp. 371 - 375
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

Beale, S. I. and Weinstein, J. D. 1990. Tetrapyrrole metabolism in photosynthetic organisms. Pages 287–391. in Dailey, H. A. Biosynthesis of Heme and Chlorophylls. New York McGraw-Hill.Google Scholar
Chow, K. S., Singh, D. P., Roper, J. M., and Smith, A. G. 1997. A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria. J. Biol. Chem. 272:27,565–27,571.Google Scholar
Diggle, A. and Neve, P. 2001. The population dynamics and genetics of herbicide resistance—a modeling approach. Pages 62–96. in Powles, S. and Shaner, D. Herbicide Resistance and World Grains. Boca Raton, FL CRC.Google Scholar
Doyle, J. J. and Doyle, J. L. 1990. Isolation of plant DNA from fresh tissue. Focus. 12:13–15.Google Scholar
Gressel, J. and Levy, A. 2006. Agriculture: the selector of improbable mutations. Proc. Natl. Acad. Sci. U.S.A. 103:12,215–12,216.Google Scholar
Gressel, J. and Segel, L. 1978. The paucity of plants evolving genetic resistance to herbicides: possible reasons and implications. J. Theor. Biol. 75:349–371.Google Scholar
Gressel, J. and Segel, L. 1990. Modeling the effectiveness of herbicide rotations and mixtures as strategies to delay or preclude resistance. Weed Technol. 4:186–198.CrossRefGoogle Scholar
Heap, I. 2007. International Survey of Herbicide Resistant Weeds. http://www.weedscience.com. Accessed: November 30, 2007.Google Scholar
Jacobs, J. M. and Jacobs, N. J. 1984. Protoporphyrinogen oxidation, an enzymatic step in heme and chlorophyll synthesis: partial characterization of the reaction in plant organelles and comparison with mammalian and bacterial systems. Arch. Biochem. Biophys. 218:233–239.Google Scholar
Jacobs, J. M., Jacobs, N., Sherman, T. D., and Duke, S. 1991. Effect of diphenyl ether herbicides on oxidation of protoporphyrinogen to protoporphyrin in organellar and plasma membrane enriched fractions of barley. Plant Physiol. 97:197–203.CrossRefGoogle ScholarPubMed
Jacobs, J. M. and Jacobs, N. J. 1993. Porphyrin accumulation and export by isolated barley (Hordeum vulgare) plastids (effect of diphenyl ether herbicides). Plant Physiol. 101:1181–1187.CrossRefGoogle ScholarPubMed
Lee, H. J. and Duke, S. O. 1994. Protoporphyrinogen IX-oxidizing activities involved in the mode of action of peroxidizing herbicides. J. Agric. Food Chem. 42:2610–2618.Google Scholar
Lee, H. J., Lee, S. B., Chung, J. S., Han, S. U., Han, O., Guh, J. O., Jeon, J. S., An, G., and Back, K. 2000. Transgenic rice plants expressing a Bacillus subtilis protoporphyrinogen oxidase gene are resistant to diphenyl ether herbicide oxyfluorfen. Plant Cell Physiol. 41:743–749.Google Scholar
Lermontova, I. and Grimm, B. 2000. Overexpression of plastidic protoporphyrinogen IX oxidase leads to resistance to the diphenyl-ether herbicide acifluorfen. Plant Physiol. 122:75–83.Google Scholar
Lermontova, I., Kruse, E., Mock, H. P., and Grimm, B. 1997. Cloning and characterization of a plastidal and a mitochondrial isoform of tobacco protoporphyrinogen IX oxidase. Proc. Natl. Acad. Sci. U.S.A. 94:8895–8900.Google Scholar
Matsunaka, S. 1976. Diphenyl ethers. Pages 709–739. in Kearney, P. C. and Kaufman, D. D. Herbicides: Chemistry, Degradation, and Mode of Action. Volume 2. New York Marcel Dekker.Google Scholar
Maxwell, B., Roush, M., and Radosevich, S. 1990. Predicting the evolution and dynamics of herbicide resistance in weed populations. Weed Technol. 4:2–14.Google Scholar
Patzoldt, W. L., Hager, A. G., McCormick, J. S., and Tranel, P. J. 2006. A codon deletion confers resistance to herbicides inhibiting protoporphyrinogen oxidase. Proc. Natl. Acad. Sci. U.S.A. 103:12,329–12,334.Google Scholar
Smith, A. G., Marsh, O., and Elder, G. H. 1993. Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem. J. 292:502–508.Google Scholar
Watanabe, N., Che, F. S., Iwano, M., Takayama, S., and Yoshida, S. 2001. Dual targeting of spinach protoporphyrinogen oxidase II to mitochondria and chloroplasts by alternative use of two in-frame initiation codons. J. Biol. Chem. 276:20,474–20,481.Google Scholar