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dc.contributor.authorPustelny, Christian
dc.contributor.authorBrouwer, Stephan
dc.contributor.authorMüsken, Mathias
dc.contributor.authorBielecka, Agata
dc.contributor.authorDötsch, Andreas
dc.contributor.authorNimtz, Manfred
dc.contributor.authorHäussler, Susanne
dc.date.accessioned2013-05-31T11:03:57Z
dc.date.available2013-05-31T11:03:57Z
dc.date.issued2013-02
dc.identifier.citationThe peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14. 2013, 15 (2):597-609 Environ. Microbiol.en_GB
dc.identifier.issn1462-2920
dc.identifier.pmid23278968
dc.identifier.doi10.1111/1462-2920.12040
dc.identifier.urihttp://hdl.handle.net/10033/293149
dc.description.abstractPseudomonas 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 PA14 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 Escherichia 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 PA14_prmC mutant strain is unable to grow under anoxic conditions and has a significantly reduced pathogenicity in the infection model Galleria 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.
dc.language.isoenen
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/260276/en
dc.rightsArchived with thanks to Environmental microbiologyen_GB
dc.rightsopenAccessen
dc.titleThe peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14.en
dc.typeArticleen
dc.contributor.departmentDepartment of Molecular Bacteriology, Helmholtz Center for Infection Research, Braunschweig, Germany. Christian.pustelny@helmholtz-hzi.deen_GB
dc.identifier.journalEnvironmental microbiologyen_GB
refterms.dateFOA2014-02-15T00:00:00Z
html.description.abstractPseudomonas 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 PA14 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 Escherichia 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 PA14_prmC mutant strain is unable to grow under anoxic conditions and has a significantly reduced pathogenicity in the infection model Galleria 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.


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