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

被引:51
作者
Brunharo, Caio A. C. G. [1 ]
Takano, Hudson K. [2 ]
Mallory-Smith, Carol A. [1 ]
Dayan, Franck E. [2 ]
Hanson, Bradley D. [3 ]
机构
[1] Oregon State Univ, Dept Crop & Soil Sci, 3050 Southwest Campus Way,Crop Sci Bldg, Corvallis, OR 97331 USA
[2] Colorado State Univ, Dept Bioagr Sci & Pest Management, 1777 Campus Delivery, Ft Collins, CO 80523 USA
[3] Univ Calif Davis, Dept Plant Sci, One Shields Ave,MS-4, Davis, CA 95616 USA
关键词
enzyme modeling; gene expression; herbicide absorption; herbicide degradation; herbicide translocation; non-target site resistance; phosphinothricin; L-PHOSPHINOTHRICIN GLUFOSINATE; GOOSEGRASS ELEUSINE-INDICA; TARGET-SITE MUTATION; CELLULAR-LOCALIZATION; STRUCTURE VALIDATION; GLYPHOSATE; AMMONIUM; TRANSLOCATION; MOLPROBITY; PROTEIN;
D O I
10.1021/acs.jafc.9b01392
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Glufosinate-resistant 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.
引用
收藏
页码:8431 / 8440
页数:10
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