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Target-site resistance to acetolactate synthase inhibitors in wild mustard (Sinapis arvensis)

Published online by Cambridge University Press:  20 January 2017

Michael J. Christoffers ,
Vijay K. Nandula ,
Kirk A. Howatt  and
Todd R. Wehking
Vijay K. Nandula
Affiliation:
Department of Plant Sciences, North Dakota State University, Fargo, ND 58105
Kirk A. Howatt
Affiliation:
Department of Plant Sciences, North Dakota State University, Fargo, ND 58105
Todd R. Wehking
Affiliation:
Department of Plant Sciences, North Dakota State University, Fargo, ND 58105
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Abstract

Inhibitors of acetolactate synthase (ALS) are important herbicides for control of wild mustard, a common weed of the north central United States and Canada. Wild mustard that survived treatments with the ALS inhibitors cloransulam, imazethapyr, and thifensulfuron was sampled from a North Dakota soybean field in 1999. The mechanism of resistance and response of this wild mustard biotype to ALS-inhibiting herbicides was investigated. In vitro enzyme-inhibition experiments confirmed a resistance mechanism associated with the ALS enzyme; imazethapyr or imazamox at 1 × 10−4 M caused only 10 to 11% and 12 to 16% reductions in ALS activity, respectively. ALS from a susceptible wild mustard biotype was inhibited 50% (I50) with imazethapyr at 8 × 10−7 M or imazamox at 1.1 × 10−6 M. Whole-plant greenhouse treatments confirmed cross-resistance across ALS-inhibitor classes. Treatment with twice-normal field rates of thifensulfuron, ethametsulfuron, triflusulfuron, imazamox, imazethapyr, flumetsulam, cloransulam, flucarbazone, and imazamethabenz reduced biomass of the susceptible biotype at least 96% 28 d after treatment. Biomass of the resistant biotype was reduced 49% by triflusulfuron and 35% by thifensulfuron, but was not reduced by other herbicides. DNA sequence analysis of ALS genes from resistant and susceptible biotypes revealed a point mutation inferring a Trp-to-Leu amino acid substitution in ALS of the resistant biotype. This mutation, corresponding to position 574 of the Arabidopsis ALS amino acid sequence, is known to confer cross-resistance to ALS-inhibiting herbicides and is the probable cause of resistance in the wild mustard biotype. Phylogenetic analysis of wild mustard and canola ALS sequences confirmed that the Trp574 mutation arose within wild mustard and was not derived via introgression from imidazolinone-resistant canola. The results of this research indicate a naturally occurring target-site point mutation responsible for conferring cross-resistance to ALS-inhibiting herbicides in this wild mustard biotype.

Keywords

Cloransulam, ethametsulfuron, flucarbazone, flumetsulam, imazamethabenz, imazamox, imazethapyr, thifensulfuron, triflusulfuron, Arabidopsis, Arabidopsis thaliana (L.) Heynh., ARBTHwild mustard, Sinapis arvensis L., SINARcanola, Brassica napus L.soybean, Glycine max (L.) MerrAcetohydroxyacid synthaseALS sequencesAHASherbicide resistancetarget-site mutation
Type
Physiology, Chemistry, Biochemistry
Information
Weed Science , Volume 54 , Issue 2 , April 2006 , pp. 191 - 197
Copyright
Copyright © Weed Science Society of America 

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Footnotes

Current address: Delta Research and Extension Center, Mississippi State University, Stoneville, MS 38776
Current address: Cargill Inc., Minneapolis, MN 55440

References

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