Inhibition of O-acetylserine (thiol) lyase as a promising new mechanism of action for herbicides.

Autor: Foletto-Felipe MP; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil; Coordination of Degree in Biological Sciences, Federal Technological University of Paraná, Campus Dois Vizinhos, Paraná, Brazil., Abrahão J; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Siqueira-Soares RC; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Contesoto IC; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Grizza LHE; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., de Almeida GHG; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Constantin RP; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Philippsen GS; Federal University of Paraná, Paraná, Brazil., Seixas FAV; Department of Technology, State University of Maringá, Umuarama, Paraná, Brazil., Bueno PSA; Department of Technology, State University of Maringá, Umuarama, Paraná, Brazil., de Oliveira MAS; Laboratory of Molecular Biology of Prokaryotes, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Constantin RP; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Dos Santos WD; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Ferrarese-Filho O; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil., Marchiosi R; Laboratory of Plant Biochemistry, Department of Biochemistry, State University of Maringá, Paraná, Brazil. Electronic address: rmarchiosi@uem.br.
Jazyk: angličtina
Zdroj: Plant physiology and biochemistry : PPB [Plant Physiol Biochem] 2023 Nov; Vol. 204, pp. 108127. Date of Electronic Publication: 2023 Oct 20.
DOI: 10.1016/j.plaphy.2023.108127
Abstrakt: Enzymes of the sulfur assimilation pathway of plants have been identified as potential targets for herbicide development, given their crucial role in synthesizing amino acids, coenzymes, and various sulfated compounds. In this pathway, O-acetylserine (thiol) lyase (OAS-TL; EC 2.5.1.47) catalyzes the synthesis of L-cysteine through the incorporation of sulfate into O-acetylserine (OAS). This study used an in silico approach to select seven inhibitors for OAS-TL. The in silico experiments revealed that S-benzyl-L-cysteine (SBC) had a better docking score (-7.0 kcal mol -1 ) than the substrate OAS (-6.6 kcal mol -1 ), indicating its suitable interaction with the active site of the enzyme. In vitro experiments showed that SBC is a non-competitive inhibitor of OAS-TL from Arabidopsis thaliana expressed heterologously in Escherichia coli, with a K ic of 4.29 mM and a K iu of 5.12 mM. When added to the nutrient solution, SBC inhibited the growth of maize and morning glory weed plants due to the reduction of L-cysteine synthesis. Remarkably, morning glory was more sensitive than maize. As proof of its mechanism of action, L-cysteine supplementation to the nutrient solution mitigated the inhibitory effect of SBC on the growth of morning glory. Taken together, our data suggest that reduced L-cysteine synthesis is the primary cause of growth inhibition in maize and morning glory plants exposed to SBC. Furthermore, our findings indicate that inhibiting OAS-TL could potentially be a novel approach for herbicidal action.
Competing Interests: Declaration of competing interest The authors have no conflicts of interest.
(Copyright © 2023. Published by Elsevier Masson SAS.)
Databáze: MEDLINE
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