Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

Schönbrunn, E.; Eschenburg, Susanne; Shuttleworth, Wendy A.; Schloss, John V.; Amrhein, Nikolaus; Evans, Jeffrey S.; Kabsch, Wolfgang

doi:10.1073/pnas.98.4.1376

Cited by 473 publications

(454 citation statements)

References 33 publications

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“…By restoring the incomplete blend with synthetic compounds that are missing, the importance of the added compounds can be confirmed . Here, we used glyphosate, an inhibitor of the enzyme EPSP synthase (Haslam, 1993;Schönbrunn et al, 2001), to inhibit the production of shikimic acid derived HIPVs. As expected, this inhibitor treatment resulted in a strong reduction of the emission of indole, methyl anthranilate, phenethyl acetate, and benzyl acetate, whereas the amounts of most other compounds, except two green-leaf volatiles, were not affected by the inhibitor treatment (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Delprim) that had been fed upon by larvae of Spodoptera littoralis (Boisduval) (Lepidoptera: Noctuidae) by incubating the plants in glyphosate [N-(phosphonomethyl)-glycine]. This compound inhibits the enzyme 5-enolpyruvylshikimate-3-phospate (EPSP) synthase (Haslam, 1993;Schönbrunn et al, 2001) and strongly reduces the amounts of shikimic acid derived VOCs. Attraction of the odor from these inhibited plants was compared to that of the natural blends emitted by control plants.…”

Section: Introductionmentioning

confidence: 99%

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The Role of Indole and Other Shikimic Acid Derived Maize Volatiles in the Attraction of Two Parasitic Wasps

et al. 2006

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After herbivore attack, plants release a plethora of different volatile organic compounds (VOCs), which results in odor blends that are attractive to predators and parasitoids of these herbivores. VOCs in the odor blends emitted by maize plants (Zea mays) infested by lepidopteran larvae are well characterized. They are derived from at least three different biochemical pathways, but the relative importance of each pathway for the production of VOCs that attract parasitic wasps is unknown. Here, we studied the importance of shikimic acid derived VOCs for the attraction of females of the parasitoids Cotesia marginiventris and Microplitis rufiventris. By incubating caterpillar-infested maize plants in glyphosate, an inhibitor of the 5-enolpyruvylshikimate-3-phospate (EPSP) synthase, we obtained induced odor blends with only minute amounts of shikimic acid derived VOCs. In olfactometer bioassays, the inhibited plants were as attractive to naive C. marginiventris females as control plants that released normal amounts of shikimic acid derived VOCs, whereas naive M. rufiventris females preferred inhibited plants to control plants. By adding back synthetic indole, the quantitatively most important shikimic acid derived VOC in induced maize odors, to inhibited plants, we showed that indole had no effect on the attraction of C. marginiventris and that M. rufiventris preferred blends without synthetic indole. Exposing C. marginiventris females either to odor blends of inhibited or control plants during oviposition experiences shifted their preference in subsequent olfactometer tests in favor of the experienced odor. Further learning experiments with synthetic indole showed that C. marginiventris can learn to respond to this compound, but that this does not affect its choices between natural induced blends with or without indole. We hypothesize that for naïve wasps the attractiveness of an herbivore-induced odor blend is reduced due to masking by nonattractive compounds, and that during oviposition experiences in the presence of complex odor blends, parasitoids strongly associate some compounds, whereas others are largely ignored.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Role of Indole and Other Shikimic Acid Derived Maize Volatiles in the Attraction of Two Parasitic Wasps

et al. 2006

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“…The behavior of Tyr200 is especially interesting: as titration with S3P proceeds, its peak visibly broadens, presumably due to chemical exchange, and shifts by small degrees from its original position to its S3P-bound position. This residue is mentioned in [6,7] as one that undergoes a major conformational change upon S3P binding. Ser23 and Arg27 have been subjected to Fig.…”

Section: Discussionmentioning

confidence: 99%

“…mutagenesis (unpublished results and [15]), with 10% and undetectable residual activity, respectively, for the alanine substitutions. Ser23 is involved in S3P binding only in the Scho « nbrunn binary complex structure [7], while Arg27 and Ser197 are implicated in both binary complex structures. Ser197 makes one hydrogen bond to S3P in the closed structure [7], but two in the open structure [6].…”

Section: Discussionmentioning

confidence: 99%

“…In 1997, Stallings et al released several pictures of their enzymeWS3P complex [6], in which the enzyme maintains an open conformation, and all contacts between S3P and the enzyme are in the N-terminal domain. More recently, Scho « nbrunn et al [7] have crystallized the binary enzyme b S3P complex in a closed conformation where S3P has multiple contacts with residues in both domains. Both structures have experimental caveats.…”

Section: Introductionmentioning

confidence: 99%

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Chemical shift mapping of shikimate‐3‐phosphate binding to the isolated N‐terminal domain of 5‐enolpyruvylshikimate‐3‐phosphate synthase

2001

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To facilitate evaluation of enzyme^ligand complexes in solution, we have isolated the 26-kDa N-terminal domain of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase for analysis by NMR spectroscopy. The isolated domain is capable of binding the substrate shikimate-3-phosphate (S3P), and this letter reports the localization of the S3P binding site using chemical shift mapping. Based on the NMR data, we propose that Ser23, Arg27, Ser197, and Tyr200 are directly involved in S3P binding. We also describe changes in the observed nuclear Overhauser effects (NOEs) that are consistent with a partial conformational change in the N-terminal domain upon S3P binding. ß

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Engineering Resistance to Herbicides

CaJacob

Feng

Heck

et al. 2004

Handbook of Plant Biotechnology

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Crop resistance can be generated through a selection process or the introduction of a gene via transformation. We will refer to the latter as engineered herbicide resistance. The literature contains numerous studies on engineered plant resistance to various herbicide classes. There is a large distinction between demonstrating a resistance phenotype in plants versus developing a commercial resistant crop that requires consistent performance under varying environmental conditions. Creating an herbicide resistant crop must successfully navigate a maze of key technical issues while satisfying the practical product goals of agronomic equivalence, weed management, economic feasibility, governmental regulatory compliance and public acceptance. Most of our experience has been derived from developing crop resistance to glyphosate. In this review, we will utilise these experiences to describe the essential studies required for the development of a commercial herbicide‐resistant crop with emphasis on the development of glyphosate resistance.

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Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail

Cited by 473 publications

References 33 publications

The Role of Indole and Other Shikimic Acid Derived Maize Volatiles in the Attraction of Two Parasitic Wasps

The Role of Indole and Other Shikimic Acid Derived Maize Volatiles in the Attraction of Two Parasitic Wasps

Chemical shift mapping of shikimate‐3‐phosphate binding to the isolated N‐terminal domain of 5‐enolpyruvylshikimate‐3‐phosphate synthase

Engineering Resistance to Herbicides

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