Is Proteomics a Reliable Tool to Probe the Oxidative Folding of Bacterial Membrane Proteins?
| Autor: | Vivianne J. Goosens, André Vente, Tjeerd van Rij, Thijs R. H. M. Kouwen, Annette Dreisbach, Jan Maarten van Dijl, Maurien M.A. Olsthoorn, Michiel Akeroyd, Emma L. Denham, Ruben A. T. Mars |
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| Přispěvatelé: | Microbes in Health and Disease (MHD), Translational Immunology Groningen (TRIGR) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Proteomics
Protein Folding GENES Physiology Clinical Biochemistry Mutant Bacillus subtilis Biology Biochemistry BACILLUS-SUBTILIS Bacterial Proteins Molecular Biology General Environmental Science Oxidative folding Membrane Proteins Cell Biology biology.organism_classification Membrane Membrane protein Cytoplasm General Earth and Planetary Sciences Electrophoresis Polyacrylamide Gel Protein folding |
| Zdroj: | Antioxidants & Redox Signaling, 18(10), 1159-1164. MARY ANN LIEBERT, INC |
| ISSN: | 1523-0864 |
| DOI: | 10.1089/ars.2012.4664 |
| Popis: | The oxidative folding of proteins involves disulfide bond formation, which is usually catalyzed by thiol-disulfide oxidoreductases (TDORs). In bacteria, this process takes place in the cytoplasmic membrane and other extracytoplasmic compartments. While it is relatively easy to study oxidative folding of water-soluble proteins on a proteome-wide scale, this has remained a major challenge for membrane proteins due to their high hydrophobicity. Here, we have assessed whether proteomic techniques can be applied to probe the oxidative folding of membrane proteins using the Gram-positive bacterium Bacillus subtilis as a model organism. Specifically, we investigated the membrane proteome of a B. subtilis bdbCD mutant strain, which lacks the primary TDOR pair BdbC and BdbD, by gel-free mass spectrometry. In total, 18 membrane-associated proteins showed differing behavior in the bdbCD mutant and the parental strain. These included the ProA protein involved in osmoprotection. Consistent with the absence of ProA, the bdbCD mutant was found to be sensitive to osmotic shock. We hypothesize that membrane proteomics is a potentially effective approach to profile oxidative folding of bacterial membrane proteins. Antioxid. Redox Signal. 18, 1159-1164. |
| Databáze: | OpenAIRE |
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