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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/11995

Title: A proteome analysis of the response of a Pseudomonas aeruginosa oxyR mutant to iron limitation
Authors: Vinckx, Tiffany
Wei, Qing
Matthijs, Sandra
NOBEN, Jean-Paul
DANIELS, Ruth
Cornelis, Pierre
Issue Date: 2011
Publisher: SPRINGER
Citation: BIOMETALS, 24(3). p. 523-532
Abstract: In Pseudomonas aeruginosa the response to oxidative stress is orchestrated by the LysR regulator OxyR by activation of the transcription of two catalase genes (katA and katB), of the alkyl-hydroxyperoxidases ahpCF and ahpB. Next to the expected high sensitivity to oxidative stress generated by reactive oxygen species (ROS: H2O2, O-2 (-)), the oxyR mutant shows a defective growth under conditions of iron limitation (Vinckx et al. 2008). Although production and uptake of the siderophore pyoverdine is not affected by the absence of oxyR, the mutant is unable to satisfy its need for iron when grown under iron limiting conditions. In order to get a better insight into the effects caused by iron limitation on the physiological response of the oxyR mutant we decided to compare the proteomes of the wild type and the mutant grown in the iron-poor casamino acids medium (CAA), in CAA plus H2O2, and in CAA plus the strong iron chelator ethylenediamine-N,N'-bis(2-hydroxyphenylacetic acid) (EDDHA). Especially in the presence of hydrogen peroxide the oxyR cells increase the production of stress proteins (Dps and IbpA). The superoxide dismutase SodM is produced in higher amounts in the oxyR mutant grown in CAA plus H2O2. The PchB protein, a isochorismate-pyruvate lyase involved in the siderophore pyochelin biosynthesis is not detectable in the extracts from the oxyR mutant grown in the presence of hydrogen peroxide. When cells were grown in the presence of EDDHA, we observed a reduction of the ferric uptake regulator (Fur), and an increase in the two subunits of the succinyl-CoA synthetase and the fumarase FumC1.
Notes: [Vinckx, Tiffany; Wei, Qing; Matthijs, Sandra; Cornelis, Pierre] Vrije Univ Brussel VIB, Dept Mol & Cell Interact, Lab Microbial Interact, B-1050 Brussels, Belgium. [Noben, Jean-Paul; Daniels, Ruth] Hasselt Univ, Biomed Res Inst, B-3590 Diepenbeek, Belgium. pcornel@vub.ac.be
URI: http://hdl.handle.net/1942/11995
DOI: 10.1007/s10534-010-9403-4
ISI #: 000290448500015
ISSN: 0966-0844
Category: A1
Type: Journal Contribution
Validation: ecoom, 2012
Appears in Collections: Research publications

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