A proteome analysis of the response of a Pseudomonas aeruginosa oxyR mutant to iron limitation
| العنوان: | A proteome analysis of the response of a Pseudomonas aeruginosa oxyR mutant to iron limitation |
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| المؤلفون: | Pierre Cornelis, Tiffany Vinckx, Qing Wei, Ruth Daniels, Jean-Paul Noben, Sandra Matthijs |
| المصدر: | BioMetals. 24:523-532 |
| بيانات النشر: | Springer Science and Business Media LLC, 2011. |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | Siderophore, Proteome, Iron, Mutant, General Biochemistry, Genetics and Molecular Biology, Biomaterials, Superoxide dismutase, chemistry.chemical_compound, Tandem Mass Spectrometry, Electrophoresis, Gel, Two-Dimensional, chemistry.chemical_classification, Reactive oxygen species, Pyoverdine, biology, Metals and Alloys, Wild type, EDDHA, chemistry, Biochemistry, Catalase, Pseudomonas aeruginosa, Trans-Activators, biology.protein, bacteria, General Agricultural and Biological Sciences, Chromatography, Liquid |
| الوصف: | 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: H(2)O(2), 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 H(2)O(2), 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 H(2)O(2). 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. |
| تدمد: | 1572-8773 0966-0844 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::341830da8e917a996cae8aec5a10dabf https://doi.org/10.1007/s10534-010-9403-4 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....341830da8e917a996cae8aec5a10dabf |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. | تدمد: | 15728773 09660844 |
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