Structural basis of resistance to herbicides that target acetohydroxyacid synthase

Thierry Lonhienne, Yan Cheng, Mario D. Garcia, Shu Hong Hu, Yu Shang Low, Gerhard Schenk, Craig M. Williams and Luke W. Guddat ()
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Thierry Lonhienne: The University of Queensland
Yan Cheng: The University of Queensland
Mario D. Garcia: The University of Queensland
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

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-31023-x

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