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- W1947724021 abstract "Summary P seudomonas aeruginosa pathogenicity and its capability to adapt to multiple environments are dependent on the production of diverse virulence factors, controlled by the sophisticated quorum sensing ( QS ) network of P . aeruginosa . To better understand the molecular mechanisms that underlie this adaptation we searched for novel key regulators of virulence factor production by screening a PA 14 transposon mutant library for potential candidates acting downstream of the unique 2‐alkyl‐4‐quinolone ( AQ ) QS system of P . aeruginosa . We focused the work on a protein named HemK with high homology to PrmC of E scherichia coli displaying a similar enzymatic activity (therefore also referred to as PrmC ). In this study, we demonstrate that PrmC is an S ‐adenosyl‐ l ‐methionine ( AdoMet )‐dependent methyltransferase of peptide chain release factors ( RFs ) essential for the expression of several virulence factors, such as pyocyanin, rhamnolipids and the type III ‐secreted toxin ExoT . Furthermore, the PA 14_ prmC mutant strain is unable to grow under anoxic conditions and has a significantly reduced pathogenicity in the infection model G alleria mellonella . Along with transcriptomic and proteomic analyses, the presented data indicate that the methylation of RFs in P . aeruginosa seems to have a global effect on cellular processes related to the virulence of this nosocomial pathogen." @default.
- W1947724021 created "2016-06-24" @default.
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- W1947724021 date "2012-12-28" @default.
- W1947724021 modified "2023-09-25" @default.
- W1947724021 title "The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of<i>Pseudomonas aeruginosa</i>PA14" @default.
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- W1947724021 doi "https://doi.org/10.1111/1462-2920.12040" @default.
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