We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Glyphosate-Induced Phosphonatase Operons in Soil Bacteria of the Genus Achromobacter.
- Authors
Epiktetov, Dmitry O.; Sviridov, Alexey V.; Tarlachkov, Sergey V.; Shushkova, Tatyana V.; Toropygin, Ilya Yu.; Leontievsky, Alexey A.
- Abstract
Achromobacter insolitus and Achromobacter aegrifaciens, bacterial degraders of the herbicide glyphosate, were found to induce phosphonatase (phosphonoacetaldehyde hydrolase, EC 3.11.1.1) when grown on minimal media with glyphosate as the sole source of phosphorus. The phosphonatases of the strains were purified to an electrophoretically homogeneous state and characterized. The enzymes differed in their kinetic characteristics and some other parameters from the previously described phosphonatases. The phosphonatase of A. insolitus was first revealed to separate into two stable forms, which had similar kinetic characteristics but interacted differently with affinity and ion-exchange resins. The genomes of the investigated bacteria were sequenced. The phosphonatase genes were identified, and their context was determined: the bacteria were shown to have gene clusters, which, besides the phosphonatase operon, included genes for LysR-type transcription activator (substrate sensor) and putative iron-containing oxygenase PhnHD homologous to monooxygenases PhnY and TmpB of marine organophosphonate degraders. Genes of 2-aminoethylphosphonate aminotransferase (PhnW, EC 2.6.1.37) were absent in the achromobacterial phosphonatase operons; instead, we revealed the presence of genes encoding the putative flavin oxidase HpnW. In silico simulation showed 1-hydroxy-2-aminoethylphosphonate to be the most likely substrate of the new monooxygenase, and a number of glycine derivatives structurally similar to glyphosate to be substrates of flavin oxidase.
- Subjects
BACTERIAL operons; SOIL microbiology; OPERONS; ACHROMOBACTER; BACTERIAL genomes; GLYPHOSATE; IRON
- Publication
International Journal of Molecular Sciences, 2024, Vol 25, Issue 12, p6409
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms25126409