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Identification of the first glyphosate transporter by genomic adaptation
Author(s) -
Wicke Dennis,
Schulz Lisa M.,
Lentes Sabine,
Scholz Patricia,
Poehlein Anja,
Gibhardt Johannes,
Daniel Rolf,
Ischebeck Till,
Commichau Fabian M.
Publication year - 2019
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.14534
Subject(s) - biology , bacillus subtilis , biochemistry , glyphosate , glycine , symporter , transporter , glutamine , mutant , escherichia coli , amino acid , bacteria , gene , genetics , microbiology and biotechnology
Summary The soil bacterium Bacillus subtilis can get into contact with growth‐inhibiting substances, which may be of anthropogenic origin. Glyphosate is such a substance serving as a nonselective herbicide. Glyphosate specifically inhibits the 5‐enolpyruvyl‐shikimate‐3‐phosphate (EPSP) synthase, which generates an essential precursor for de novo synthesis of aromatic amino acids in plants, fungi, bacteria and archaea. Inhibition of the EPSP synthase by glyphosate results in depletion of the cellular levels of aromatic amino acids unless the environment provides them. Here, we have assessed the potential of B. subtilis to adapt to glyphosate at the genome level. In contrast to Escherichia coli , which evolves glyphosate resistance by elevating the production and decreasing the glyphosate sensitivity of the EPSP synthase, B. subtilis primarily inactivates the gltT gene encoding the high‐affinity glutamate/aspartate symporter GltT. Further adaptation of the gltT mutants to glyphosate led to the inactivation of the gltP gene encoding the glutamate transporter GltP. Metabolome analyses confirmed that GltT is the major entryway of glyphosate into B. subtilis . GltP, the GltT homologue of E. coli also transports glyphosate into B. subtilis . Finally, we found that GltT is involved in uptake of the herbicide glufosinate, which inhibits the glutamine synthetase.