A new version of this entry is available:

Abstract (English)

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.

File is subject to an embargo until

This is a new version of:

Notes

Publication license

Publication series

Published in

Environmental microbiology, 25 (2023), 12, 3604-3622. https://doi.org/10.1111/1462-2920.16518. ISSN: 1462-2920
Faculty
Institute

Examination date

Supervisor

Edition / version

Citation

DOI

ISSN

ISBN

Language
English

Publisher

Publisher place

Classification (DDC)
570 Biology

Original object

Standardized keywords (GND)

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}, }