Revealing novel protein interaction partners of glyphosate in Escherichia coli
Despite all debates about its safe use, glyphosate remains the most widely applied active ingredient in herbicide products, with renewed approval in the European Union until 2033. Non-target organisms are commonly exposed to glyphosate as a matter of its mode of application, with its broader environ...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-01-01
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| Series: | Environment International |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0160412024008304 |
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| author | Alix Sarah Aldehoff Dominique Türkowsky Patrick Lohmann Masun Nabhan Homsi Ulrike Rolle–Kampczyk Elke Ueberham Jörg Lehmann Martin von Bergen Nico Jehmlich Sven–Bastiaan Haange |
| author_facet | Alix Sarah Aldehoff Dominique Türkowsky Patrick Lohmann Masun Nabhan Homsi Ulrike Rolle–Kampczyk Elke Ueberham Jörg Lehmann Martin von Bergen Nico Jehmlich Sven–Bastiaan Haange |
| author_sort | Alix Sarah Aldehoff |
| collection | DOAJ |
| description | Despite all debates about its safe use, glyphosate remains the most widely applied active ingredient in herbicide products, with renewed approval in the European Union until 2033. Non-target organisms are commonly exposed to glyphosate as a matter of its mode of application, with its broader environmental and biological impacts remaining under investigation. Glyphosate displays structural similarity to phosphoenolpyruvate (PEP), thereby competitively inhibiting the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), crucial for the synthesis of aromatic amino acids in plants, fungi, bacteria, and archaea. Most microbes, including the gut bacterium Escherichia coli (E. coli), possess a glyphosate-sensitive class I EPSPS, making them vulnerable to glyphosate’s effects. Yet, little is known about glyphosate’s interactions with other bacterial proteins or its broader modes of action at the proteome level. Here, we employed a quantitative proteomics and thermal proteome profiling (TPP) approach to identify novel protein binding partners of glyphosate in the E. coli proteome. Glyphosate exposure significantly altered amino acid synthesizing pathways. The abundance of shikimate pathway proteins was increased, suggesting a compensatory mechanism. Extracellular riboflavin concentrations were elevated upon glyphosate exposure, while intracellular levels remained stable. Beyond the target enzyme EPSPS, thermal proteome profiling indicated an effect of glyphosate on the thermal stability of certain proteins, including AroH and ProA, indicating interactions. Similar to the competitive binding between PEP and glyphosate at EPSPS, one reason for the interaction of AroH and ProA with the herbicide could be a high structural similarity between their substrates and glyphosate. Overall, glyphosate induced metabolic disturbances in E. coli, extending beyond its primary target, thereby providing new insights into glyphosate’s broader impact on microbial systems. |
| format | Article |
| id | doaj-art-1ee2e98296804912934ef851b8e28da2 |
| institution | Kabale University |
| issn | 0160-4120 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Environment International |
| spelling | doaj-art-1ee2e98296804912934ef851b8e28da22025-01-24T04:44:12ZengElsevierEnvironment International0160-41202025-01-01195109243Revealing novel protein interaction partners of glyphosate in Escherichia coliAlix Sarah Aldehoff0Dominique Türkowsky1Patrick Lohmann2Masun Nabhan Homsi3Ulrike Rolle–Kampczyk4Elke Ueberham5Jörg Lehmann6Martin von Bergen7Nico Jehmlich8Sven–Bastiaan Haange9Department of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyFraunhofer Institute for Cell Therapy and Immunology IZI, Department Preclinical Development and Validation, Leipzig, GermanyFraunhofer Institute for Cell Therapy and Immunology IZI, Department Preclinical Development and Validation, Leipzig, Germany; Fraunhofer Cluster of Excellence Immune-Mediated Diseases CIMD, Leipzig-Frankfurt-Hannover, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, Germany; Institute of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, Leipzig, Germany; German Centre for Integrative Biodiversity Research (iDiv) Halle-Jena-Leipzig, Leipzig, GermanyDepartment of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, Germany; Corresponding author.Department of Molecular Toxicology, Helmholtz-Centre for Environmental Research GmbH (UFZ), Leipzig, GermanyDespite all debates about its safe use, glyphosate remains the most widely applied active ingredient in herbicide products, with renewed approval in the European Union until 2033. Non-target organisms are commonly exposed to glyphosate as a matter of its mode of application, with its broader environmental and biological impacts remaining under investigation. Glyphosate displays structural similarity to phosphoenolpyruvate (PEP), thereby competitively inhibiting the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), crucial for the synthesis of aromatic amino acids in plants, fungi, bacteria, and archaea. Most microbes, including the gut bacterium Escherichia coli (E. coli), possess a glyphosate-sensitive class I EPSPS, making them vulnerable to glyphosate’s effects. Yet, little is known about glyphosate’s interactions with other bacterial proteins or its broader modes of action at the proteome level. Here, we employed a quantitative proteomics and thermal proteome profiling (TPP) approach to identify novel protein binding partners of glyphosate in the E. coli proteome. Glyphosate exposure significantly altered amino acid synthesizing pathways. The abundance of shikimate pathway proteins was increased, suggesting a compensatory mechanism. Extracellular riboflavin concentrations were elevated upon glyphosate exposure, while intracellular levels remained stable. Beyond the target enzyme EPSPS, thermal proteome profiling indicated an effect of glyphosate on the thermal stability of certain proteins, including AroH and ProA, indicating interactions. Similar to the competitive binding between PEP and glyphosate at EPSPS, one reason for the interaction of AroH and ProA with the herbicide could be a high structural similarity between their substrates and glyphosate. Overall, glyphosate induced metabolic disturbances in E. coli, extending beyond its primary target, thereby providing new insights into glyphosate’s broader impact on microbial systems.http://www.sciencedirect.com/science/article/pii/S0160412024008304GlyphosateEscherichia coliAcute and chronic exposureThermal proteome profilingProtein interaction partner |
| spellingShingle | Alix Sarah Aldehoff Dominique Türkowsky Patrick Lohmann Masun Nabhan Homsi Ulrike Rolle–Kampczyk Elke Ueberham Jörg Lehmann Martin von Bergen Nico Jehmlich Sven–Bastiaan Haange Revealing novel protein interaction partners of glyphosate in Escherichia coli Environment International Glyphosate Escherichia coli Acute and chronic exposure Thermal proteome profiling Protein interaction partner |
| title | Revealing novel protein interaction partners of glyphosate in Escherichia coli |
| title_full | Revealing novel protein interaction partners of glyphosate in Escherichia coli |
| title_fullStr | Revealing novel protein interaction partners of glyphosate in Escherichia coli |
| title_full_unstemmed | Revealing novel protein interaction partners of glyphosate in Escherichia coli |
| title_short | Revealing novel protein interaction partners of glyphosate in Escherichia coli |
| title_sort | revealing novel protein interaction partners of glyphosate in escherichia coli |
| topic | Glyphosate Escherichia coli Acute and chronic exposure Thermal proteome profiling Protein interaction partner |
| url | http://www.sciencedirect.com/science/article/pii/S0160412024008304 |
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