We report an interaction between poxA, encoding a paralog of lysyl tRNA-synthetase, and the closely linked yjeK gene, encoding a putative 2,3-β-lysine aminomutase, that is critical for virulence and stress resistance in Salmonella enterica. Salmonella poxA and yjeK mutants share extensive phenotypic pleiotropy, including attenuated virulence in mice, an increased ability to respire under nutrient-limiting conditions, hypersusceptibility to a variety of diverse growth inhibitors, and altered expression of multiple proteins, including several encoded on the SPI-1 pathogenicity island. PoxA mediates posttranslational modification of bacterial elongation factor P (EF-P), analogous to the modification of the eukaryotic EF-P homolog, eIF5A, with hypusine. The modification of EF-P is a mechanism of regulation whereby PoxA acts as an aminoacyl-tRNA synthetase that attaches an amino acid to a protein resembling tRNA rather than to a tRNA.
Navarre, W.W., Zou, S., Roy, H., Xie, J.L., Savchenko, A., Singer, A., Edvokimova, E., Prost, L.R., Kumar, R., Ibba, M. Fang, F.C. (2010) PoxA, YjeK and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica. Mol. Cell 39, 209-221. https://doi.org10.1016/j.molcel.2010.06.021
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons