4.7 Article

A novel amino acid substitution Ala-122-Tyr in ALS confers high-level and broad resistance across ALS-inhibiting herbicides

Journal

PEST MANAGEMENT SCIENCE
Volume 68, Issue 8, Pages 1164-1170

Publisher

WILEY-BLACKWELL
DOI: 10.1002/ps.3278

Keywords

acetolactate synthase (ALS); ALS-inhibiting herbicide; ALS resistance mutation; cross-resistance; wild radish (Raphanus raphanistrum L; )

Funding

  1. Grains Research and Development Corporation of Australia

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BACKGROUND: Wild radish, a problem weed worldwide, is a severe dicotyledonous weed in crops. In Australia, sustained reliance on ALS-inhibiting herbicides to control this species has led to the evolution of many resistant populations endowed by any of several ALS mutations. The molecular basis of ALS-inhibiting herbicide resistance in a novel resistant population was studied. RESULTS: ALS gene sequencing revealed a previously unreported substitution of Tyr for Ala at amino acid position 122 in resistant individuals of a wild radish population (WARR30). A purified subpopulation individually homozygous for the Ala-122-Tyr mutation was generated and characterised in terms of its response to the different chemical classes of ALS-inhibiting herbicides. Whole-plant dose-response studies showed that the purified subpopulation was highly resistant to chlorsulfuron, metosulam and imazamox, with LD50 or GR50 R/S ratio of > 1024, > 512 and > 137 respectively. The resistance to imazypyr was found to be relatively moderate (but still substantial), with LD50 and GR50 R/S ratios of > 16 and > 7.8 respectively. In vitro ALS activity assays showed that Ala-122-Tyr ALS was highly resistant to all tested ALS-inhibiting herbicides. CONCLUSION: The molecular basis of ALS-inhibiting herbicide resistance in wild radish population WARR30 was identified to be due to an Ala-122-Tyr mutation in the ALS gene. This is the first report of an amino acid substitution at Ala-122 in the plant ALS that confers high-level and broad-spectrum resistance to ALS-inhibiting herbicides, a remarkable contrast to the known mutation Ala-122-Thr endowing resistance to imidazolinone herbicide. Copyright (c) 2012 Society of Chemical Industry

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