Detoxification mechanism of herbicide in Polypogon fugax and its influence on rhizosphere enzyme activities

The excessive use of chemical herbicides has resulted in evolution of herbicide-resistant weeds. Cytochrome P450 monooxygenases (P450s) are vital detoxification enzymes for herbicide-resistant weeds. Herein, we confirmed a resistant (R) Polypogon fugax population showing resistance to quizalofop-p-ethyl, acetolactate synthase (ALS)-inhibiting herbicide pyroxsulam, and several other ACCase (acetyl-CoA carboxylase)-inhibiting herbicides. Molecular analysis revealed no target-site gene mutations in the R population. Foliar spraying with malathion clearly reversed the quizalofop-p-ethyl phytotoxicity. Higher level of quizalofop-p-ethyl degradation was confirmed in the R population using HPLC analysis. Subsequently, RNA-Seq transcriptome analysis indicated that the overexpression of CYP89A2 gene appeared to be responsible for reducing quizalofop-p-ethyl phytotoxicity. The molecular docking results supported a metabolic effect of CYP89A2 protein on most herbicides tested. Furthermore, we found that low doses of herbicides stimulated the rhizosphere enzyme activities in P. fugax and the increase of rhizosphere dehydrogenase of R population may be related to its resistance mechanism. In summary, our research has shown that metabolic herbicide resistance mediated by CYP89A2, contributes to quizalofop-p-ethyl resistance in P. fugax.

Automated summary

The excessive use of chemical herbicides has led to the evolution of herbicide-resistant weeds. Cytochrome P450 monooxygenases (P450s) play a vital role in detoxification of herbicide-resistant weeds. A resistant population of Polypogon fugax (R population) was found to be resistant to quizalofop-p-ethyl, pyroxsulam, and several other herbicides. Molecular analysis revealed no target-site gene mutations in the R population. The overexpression of the CYP89A2 gene was found to be responsible for reducing quizalofop-p-ethyl phytotoxicity.