Protein aggregation in a mutant deficient in yajL, the bacterial homolog of the Parkinsonism-associated protein DJ-1
| Autor: | Ahmed Landoulsi, Gilbert Richarme, Teresa Caldas, Fatoum Kthiri, Valérie Gautier, Phillippe Bouloc, Hai-Tuong Le, Chantal Bohn, Abderrahim Malki |
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| Přispěvatelé: | Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biochimie et Biologie Moléculaire - 03/UR/0902, Faculté des Sciences de Bizerte, Faculté des Sciences de Bizerte [Université de Carthage], Université de Carthage - University of Carthage-Université de Carthage - University of Carthage, Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Faculté des Sciences de Bizerte |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Ribosomal Proteins
Protein Folding Protein DJ-1 Protein Conformation Ribosomal Protein L3 Protein Deglycase DJ-1 Mutant Citrate (si)-Synthase Protein aggregation Biochemistry Superoxide dismutase 03 medical and health sciences Ribosomal protein Escherichia coli Humans Anaerobiosis Molecular Biology 030304 developmental biology Oncogene Proteins 2. Zero hunger chemistry.chemical_classification 0303 health sciences Reactive oxygen species biology ATP synthase Superoxide Dismutase Escherichia coli Proteins 030302 biochemistry & molecular biology Intracellular Signaling Peptides and Proteins [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Gene Expression Regulation Bacterial Hydrogen Peroxide Cell Biology Catalase Aerobiosis Oxidative Stress chemistry Chaperone (protein) Mutation Protein Structure and Folding biology.protein Reactive Oxygen Species |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (14), pp.10328-36. ⟨10.1074/jbc.M109.077529⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M109.077529⟩ |
| Popis: | International audience; YajL is the closest prokaryotic homolog of the parkinsonism-associated protein DJ-1 (40% sequence identity and similar three-dimensional structure), a protein of unknown function involved in the cellular response to oxidative stress. We report here that a yajL mutant of Escherichia coli displays an increased sensitivity to oxidative stress. It also exhibits a protein aggregation phenotype in aerobiosis, but not in anaerobiosis or in aerobic cells overexpressing superoxide dismutase, suggesting that protein aggregation depends on the presence of reactive oxygen species produced by respiratory chains. The protein aggregation phenotype of the yajL mutant, which can be rescued by the wild-type yajL gene, but not by the corresponding cysteine 106 mutant allele, is similar to that of multiple mutants deficient in superoxide dismutases and catalases, although intracellular hydrogen peroxide levels were not increased in the yajL mutant, suggesting that protein aggregation in this strain does not result from a hydrogen peroxide detoxification defect. Aggregation-prone proteins included 17 ribosomal proteins, the ATP synthase beta subunit, flagellin, and the outer membrane proteins OmpA and PAL; all of them are part of multiprotein complexes, suggesting that YajL might be involved in optimal expression of these complexes, especially during oxidative stress. YajL stimulated the renaturation of urea-unfolded citrate synthase and the solubilization of the urea-unfolded ribosomal proteins S1 and L3 and was more efficient as a chaperone in its oxidized form than in its reduced form. The mRNA levels of several aggregated proteins of the yajL mutant were severely affected, suggesting that YajL also acts at the level of gene expression. These two functions of YajL might explain the protein aggregation phenotype of the yajL mutant. |
| Databáze: | OpenAIRE |
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