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The low mutational flexibility of the EPSP synthase in Bacillus subtilis is due to a higher demand for shikimate pathway intermediates.
Schwedt, Inge; Schöne, Kerstin; Eckert, Maike; Pizzinato, Manon; Winkler, Laura; Knotkova, Barbora; Richts, Björn; Hau, Jann-Louis; Steuber, Julia; Mireles, Raul; Noda-Garcia, Lianet; Fritz, Günter; Mittelstädt, Carolin; Hertel, Robert; Commichau, Fabian M.
Affiliation
  • Schwedt I; FG Molecular Microbiology, Institute for Biology, University of Hohenheim, Stuttgart, Germany.
  • Schöne K; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.
  • Eckert M; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.
  • Pizzinato M; FG Molecular Microbiology, Institute for Biology, University of Hohenheim, Stuttgart, Germany.
  • Winkler L; FG Molecular Microbiology, Institute for Biology, University of Hohenheim, Stuttgart, Germany.
  • Knotkova B; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.
  • Richts B; Department of General Microbiology, Institute of Microbiology and Genetics, GZMB, Georg-August University of Göttingen, Göttingen, Germany.
  • Hau JL; Department of General Microbiology, Institute of Microbiology and Genetics, GZMB, Georg-August University of Göttingen, Göttingen, Germany.
  • Steuber J; FG Cellular Microbiology, Institute of Biology, University of Hohenheim, Stuttgart, Germany.
  • Mireles R; FG Cellular Microbiology, Institute of Biology, University of Hohenheim, Stuttgart, Germany.
  • Noda-Garcia L; Department of Plant Pathology and Microbiology, Hebrew University, Rehovot, Israel.
  • Fritz G; Department of Plant Pathology and Microbiology, Hebrew University, Rehovot, Israel.
  • Mittelstädt C; FG Cellular Microbiology, Institute of Biology, University of Hohenheim, Stuttgart, Germany.
  • Hertel R; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.
  • Commichau FM; FG Synthetic Microbiology, Institute for Biotechnology, BTU Cottbus-Senftenberg, Senftenberg, Germany.
Environ Microbiol ; 25(12): 3604-3622, 2023 Dec.
Article in En | MEDLINE | ID: mdl-37822042
Glyphosate (GS) inhibits the 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase that is required for aromatic amino acid, folate and quinone biosynthesis in Bacillus subtilis and Escherichia coli. The inhibition of the EPSP synthase by GS depletes the cell of these metabolites, resulting in cell death. Here, we show that like the laboratory B. subtilis strains also environmental and undomesticated isolates adapt to GS by reducing herbicide uptake. Although B. subtilis possesses a GS-insensitive EPSP synthase, the enzyme is strongly inhibited by GS in the native environment. Moreover, the B. subtilis EPSP synthase mutant was only viable in rich medium containing menaquinone, indicating that the bacteria require a catalytically efficient EPSP synthase under nutrient-poor conditions. The dependency of B. subtilis on the EPSP synthase probably limits its evolvability. In contrast, E. coli rapidly acquires GS resistance by target modification. However, the evolution of a GS-resistant EPSP synthase under non-selective growth conditions indicates that GS resistance causes fitness costs. Therefore, in both model organisms, the proper function of the EPSP synthase is critical for the cellular viability. This study also revealed that the uptake systems for folate precursors, phenylalanine and tyrosine need to be identified and characterized in B. subtilis.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacillus subtilis / 3-Phosphoshikimate 1-Carboxyvinyltransferase Language: En Journal: Environ Microbiol Journal subject: MICROBIOLOGIA / SAUDE AMBIENTAL Year: 2023 Document type: Article Affiliation country: Germany Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacillus subtilis / 3-Phosphoshikimate 1-Carboxyvinyltransferase Language: En Journal: Environ Microbiol Journal subject: MICROBIOLOGIA / SAUDE AMBIENTAL Year: 2023 Document type: Article Affiliation country: Germany Country of publication: United kingdom