A Novel Single-Site Mutation in the Catalytic Domain of Protoporphyrinogen Oxidase IX (PPO) Confers Resistance to PPO-Inhibiting Herbicides
| Autor: | Thomas Mietzner, Gulab Rangani, Michael Knapp, Nilda Roma-Burgos, Ian R. Craig, Ana Claudia Langaro, Aimone Porri, Raphael Aponte, Matheus M. Noguera, Reiofeli Salas-Perez |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
computational modeling Population Mutant PPO inhibitors Plant Science lcsh:Plant culture 01 natural sciences Palmer amaranth lcsh:SB1-1110 education Original Research education.field_of_study Acetolactate synthase biology Chemistry Amaranthus palmeri target-site resistance Wild type 04 agricultural and veterinary sciences biology.organism_classification protoporphyrinogen oxidase Biochemistry Glycine 040103 agronomy & agriculture biology.protein 0401 agriculture forestry and fisheries Protoporphyrinogen oxidase Weed cross-resistance PPO mutation 010606 plant biology & botany |
| Zdroj: | Frontiers in Plant Science, Vol 10 (2019) Frontiers in Plant Science |
| DOI: | 10.3389/fpls.2019.00568/full |
| Popis: | Protoporphyrinogen oxidase (PPO)-inhibiting herbicides are used to control weeds in a variety of crops. These herbicides inhibit heme and photosynthesis in plants. PPO-inhibiting herbicides are used to control Amaranthus palmeri (Palmer amaranth) especially those with resistance to glyphosate and acetolactate synthase (ALS) inhibiting herbicides. While investigating the basis of high fomesafen-resistance in A. palmeri, we identified a new amino acid substitution of glycine to alanine in the catalytic domain of PPO2 at position 399 (G399A) (numbered according to the protein sequence of A. palmeri). G399 is highly conserved in the PPO protein family across eukaryotic species. Through combined molecular, computational, and biochemical approaches, we established that PPO2 with G399A mutation has reduced affinity for several PPO-inhibiting herbicides, possibly due to steric hindrance induced by the mutation. This is the first report of a PPO2 amino acid substitution at G399 position in a field-selected weed population of A. palmeri. The mutant A. palmeri PPO2 showed high-level in vitro resistance to different PPO inhibitors relative to the wild type. The G399A mutation is very likely to confer resistance to other weed species under selection imposed by the extensive agricultural use of PPO-inhibiting herbicides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|