The low mutational flexibility of the EPSP synthase in Bacillus subtilis is due to a higher demand for shikimate pathway intermediates

dc.contributor.authorSchwedt, Inge
dc.contributor.authorSchöne, Kerstin
dc.contributor.authorEckert, Maike
dc.contributor.authorPizzinato, Manon
dc.contributor.authorWinkler, Laura
dc.contributor.authorKnotkova, Barbora
dc.contributor.authorRichts, Björn
dc.contributor.authorHau, Jann-Louis
dc.contributor.authorSteuber, Julia
dc.contributor.authorMireles, Raul
dc.contributor.authorNoda‐Garcia, Lianet
dc.contributor.authorFritz, Günter
dc.contributor.authorMittelstädt, Carolin
dc.contributor.authorHertel, Robert
dc.contributor.authorCommichau, Fabian M.
dc.date.accessioned2024-07-05T12:25:35Z
dc.date.available2024-07-05T12:25:35Z
dc.date.issued2023
dc.date.updated2024-06-27T03:45:02Z
dc.description.abstractGlyphosate (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.en
dc.identifier10.1111/1462-2920.16518en
dc.identifierEMI16518en
dc.identifier.urihttps://doi.org/10.1111/1462-2920.16518
dc.identifier.urihttps://hohpublica.uni-hohenheim.de/handle/123456789/15907
dc.language.isoeng
dc.relation.ispartofEnvironmental Microbiologyen
dc.rights.licensecc_by
dc.subjectGlyphosate resistance
dc.subjectEPSP synthase
dc.subjectBacillus subtilis
dc.subjectEscherichia coli
dc.subjectHerbicide uptake
dc.subjectAromatic amino acids
dc.subjectFitness costs
dc.subjectTarget modification
dc.subjectBacterial adaptation
dc.subject.ddc570
dc.titleThe low mutational flexibility of the EPSP synthase in Bacillus subtilis is due to a higher demand for shikimate pathway intermediatesen
dc.type.diniArticle
dcterms.bibliographicCitationEnvironmental microbiology, 25 (2023), 12, 3604-3622. https://doi.org/10.1111/1462-2920.16518. ISSN: 1462-2920
dcterms.bibliographicCitation.issn1462-2920
dcterms.bibliographicCitation.issue12
dcterms.bibliographicCitation.journaltitleEnvironmental microbiology
dcterms.bibliographicCitation.originalpublishernameBlackwell
dcterms.bibliographicCitation.originalpublisherplaceOxford [u.a.]
dcterms.bibliographicCitation.pageend3622
dcterms.bibliographicCitation.pagestart3604
local.export.bibtex@article{Schwedt2023, doi = {10.1111/1462-2920.16518}, author = {Schwedt, Inge and Schöne, Kerstin and Eckert, Maike et al.}, title = {The low mutational flexibility of the EPSP synthase in Bacillus subtilis is due to a higher demand for shikimate pathway intermediates}, journal = {Environmental microbiology}, year = {2023}, number = {12}, pages = {3604--3622}, }
local.export.bibtexAuthorSchwedt, Inge and Schöne, Kerstin and Eckert, Maike et al.
local.export.bibtexKeySchwedt2023
local.export.bibtexPages3604--3622
local.export.bibtexType@article

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