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Structural basis of resistance to herbicides that target acetohydroxyacid synthase

Author

Listed:
  • Thierry Lonhienne

    (The University of Queensland)

  • Yan Cheng

    (The University of Queensland)

  • Mario D. Garcia

    (The University of Queensland
    Technical University of Ambato, Tungurahua)

  • Shu Hong Hu

    (The University of Queensland)

  • Yu Shang Low

    (The University of Queensland)

  • Gerhard Schenk

    (The University of Queensland)

  • Craig M. Williams

    (The University of Queensland)

  • Luke W. Guddat

    (The University of Queensland)

Abstract

Acetohydroxyacid synthase (AHAS) is the target for more than 50 commercial herbicides; first applied to crops in the 1980s. Since then, 197 site-of-action resistance isolates have been identified in weeds, with mutations at P197 and W574 the most prevalent. Consequently, AHAS is at risk of not being a useful target for crop protection. To develop new herbicides, a functional understanding to explain the effect these mutations have on activity is required. Here, we show that these mutations can have two effects (i) to reduce binding affinity of the herbicides and (ii) to abolish time-dependent accumulative inhibition, critical to the exceptional effectiveness of this class of herbicide. In the two mutants, conformational changes occur resulting in a loss of accumulative inhibition by most herbicides. However, bispyribac, a bulky herbicide is able to counteract the detrimental effects of these mutations, explaining why no site-of-action resistance has yet been reported for this herbicide.

Suggested Citation

  • Thierry Lonhienne & Yan Cheng & Mario D. Garcia & Shu Hong Hu & Yu Shang Low & Gerhard Schenk & Craig M. Williams & Luke W. Guddat, 2022. "Structural basis of resistance to herbicides that target acetohydroxyacid synthase," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31023-x
    DOI: 10.1038/s41467-022-31023-x
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    References listed on IDEAS

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    1. Thierry Lonhienne & Yu Shang Low & Mario D. Garcia & Tristan Croll & Yan Gao & Quan Wang & Lou Brillault & Craig M. Williams & James A. Fraser & Ross P. McGeary & Nicholas P. West & Michael J. Landsbe, 2020. "Structures of fungal and plant acetohydroxyacid synthases," Nature, Nature, vol. 586(7828), pages 317-321, October.
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    Cited by:

    1. Bin Liu & Weiwu Wang & Jiguo Qiu & Xing Huang & Shenshen Qiu & Yixuan Bao & Siqiong Xu & Luyao Ruan & Tingting Ran & Jian He, 2023. "Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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