The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14.

2.50
Hdl Handle:
http://hdl.handle.net/10033/293149
Title:
The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14.
Authors:
Pustelny, Christian; Brouwer, Stephan; Müsken, Mathias; Bielecka, Agata; Dötsch, Andreas; Nimtz, Manfred; Häussler, Susanne
Abstract:
Pseudomonas 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.
Affiliation:
Department of Molecular Bacteriology, Helmholtz Center for Infection Research, Braunschweig, Germany. Christian.pustelny@helmholtz-hzi.de
Citation:
The peptide chain release factor methyltransferase PrmC is essential for pathogenicity and environmental adaptation of Pseudomonas aeruginosa PA14. 2013, 15 (2):597-609 Environ. Microbiol.
Journal:
Environmental microbiology
Issue Date:
Feb-2013
URI:
http://hdl.handle.net/10033/293149
DOI:
10.1111/1462-2920.12040
PubMed ID:
23278968
Type:
Article
Language:
en
ISSN:
1462-2920
Appears in Collections:
publications of the departmentment of molecular bacteriology(MOBA)

Full metadata record

DC FieldValue Language
dc.contributor.authorPustelny, Christianen_GB
dc.contributor.authorBrouwer, Stephanen_GB
dc.contributor.authorMüsken, Mathiasen_GB
dc.contributor.authorBielecka, Agataen_GB
dc.contributor.authorDötsch, Andreasen_GB
dc.contributor.authorNimtz, Manfreden_GB
dc.contributor.authorHäussler, Susanneen_GB
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.en_GB
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

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