NDLI: A proteome analysis of the response of a Pseudomonas aeruginosa oxyR mutant to iron limitation

Content Provider	Springer Nature Link
Author	Vinckx, Tiffany Wei, Qing Matthijs, Sandra ben, Jean Paul Daniels, Ruth Cornelis, Pierre
Copyright Year	2011
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, O2 −), 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.
Starting Page	523
Ending Page	532
Page Count	10
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	24
Issue Number	3
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2011-01-05
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pseudomonas aeruginosa oxyR Oxidative stress Iron limitation Proteome Biochemistry Physical Chemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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