PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella enterica
| Autor: | William Wiley Navarre, Jinglin L. Xie, Michael Ibba, Alex U. Singer, Hervé Roy, Lynne R. Prost, S. Betty Zou, Elena Edvokimova, Ferric C. Fang, Alexei Savchenko, Runjun D. Kumar |
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| Rok vydání: | 2010 |
| Předmět: |
Lysine-tRNA Ligase
Genomic Islands Virulence Factors Mutant Virulence Biology Article Mice chemistry.chemical_compound Bacterial Proteins Animals Molecular Biology Hypusine Genetics Lysine Salmonella enterica Drug Resistance Microbial Gene Expression Regulation Bacterial Cell Biology Peptide Elongation Factors biology.organism_classification Pathogenicity island chemistry Elongation factor P Transfer RNA Female Protein Processing Post-Translational EIF5A |
| Zdroj: | Molecular Cell. 39:209-221 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2010.06.021 |
| Popis: | We report an interaction between poxA, encoding a paralog of lysyl tRNA-synthetase, and the closely linked yjeK gene, encoding a putative 2,3-beta-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. |
| Databáze: | OpenAIRE |
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