Role of Glutamine Synthetase Isogenes and Herbicide Metabolism in the Mechanism of Resistance to Glufosinate in Lolium perenne L. spp. multiflorum Biotypes from Oregon | Zendy

Caio A. C. G. Brunharo | Zendy; Hudson Kagueyama Takano | Zendy; Carol MallorySmith | Zendy; Franck E. Dayan | Zendy; Bradley D. Hanson | Zendy

Open Access

Role of Glutamine Synthetase Isogenes and Herbicide Metabolism in the Mechanism of Resistance to Glufosinate in Lolium perenne L. spp. multiflorum Biotypes from Oregon

Author(s) -

Caio A. C. G. Brunharo,

Hudson Kagueyama Takano,

Carol MallorySmith,

Franck E. Dayan,

Bradley D. Hanson

Publication year - 2019

Publication title -

journal of agricultural and food chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.203

H-Index - 297

eISSN - 1520-5118

pISSN - 0021-8561

DOI - 10.1021/acs.jafc.9b01392

Subject(s) - glufosinate , glutamine synthetase , lolium perenne , glutamine , biology , metabolism , biochemistry , enzyme , amino acid , botany , glyphosate , agronomy , poaceae

Glufosinate-resistan Lolium perenne L. spp. multiflorum biotypes from Oregon exhibited resistance levels up to 2.8-fold the field rate. One resistant biotype (MG) had an amino acid substitution in glutamine synthetase 2 (GS2), whereas the other (OR) exhibited the wild-type genotype. We hypothesized that the amino acid substitution in GS2 is involved in the resistance mechanism in MG and that non-target site resistance mechanisms are present in OR. OR metabolized glufosinate faster than the other two biotypes, with >75% of the herbicide metabolized in comparison to 50% in MG and the susceptible biotype. A mutation in GS2 co-segregating with resistance in MG did not reduce the enzyme activity, with results further supported by our enzyme homology models. This research supports the conclusion that a metabolism mechanism of glufosinate resistance is present in OR and that glufosinate resistance in MG is not due to an altered target site.

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