YajL, the prokaryotic homolog of the Parkinsonism-associated protein DJ-1, protects cells against protein sulfenylation
| Autor: | Gilbert Richarme, Valérie Gautier, Ahmed Landoulsi, Nadia Messaoudi, Teresa Caldas, Fatoum Kthiri, Hai-Tuong Le, 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, program PHC-Utique (10G0803), Faculté des Sciences de Bizerte |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Protein Deglycase DJ-1
MESH: Escherichia coli Proteins Plasma protein binding Protein oxidation Sulfenic Acids chemistry.chemical_compound Structural Biology oxidative stress MESH: Animals Disulfides Bovine serum albumin Oncogene Proteins covalent chaperone 0303 health sciences biology MESH: Escherichia coli MESH: Protein Multimerization Escherichia coli Proteins 030302 biochemistry & molecular biology Intracellular Signaling Peptides and Proteins MESH: Ribosomal Proteins MESH: Cattle Biochemistry redox state mixed disulfides Protein Binding Ribosomal Proteins Protein DJ-1 Serum albumin MESH: Serum Albumin 03 medical and health sciences MESH: Oncogene Proteins Dihydrolipoic acid MESH: Intracellular Signaling Peptides and Proteins Escherichia coli Animals Humans MESH: Protein Binding protein oxidation MESH: Disulfides [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular Biology Serum Albumin 030304 developmental biology MESH: Humans MESH: Sulfenic Acids chemistry MESH: Protein Processing Post-Translational biology.protein Cattle Sulfenic acid Protein Multimerization Protein Processing Post-Translational |
| Zdroj: | Journal of Molecular Biology Journal of Molecular Biology, Elsevier, 2012, 421 (4-5), pp.662-70. ⟨10.1016/j.jmb.2012.01.047⟩ |
| ISSN: | 0022-2836 1089-8638 |
| DOI: | 10.1016/j.jmb.2012.01.047⟩ |
| Popis: | International audience; YajL is the closest Escherichia coli homolog of the Parkinsonism-associated protein DJ-1, a multifunctional oxidative stress response protein whose biochemical function remains unclear. We recently described the oxidative-stress-dependent aggregation of proteins in yajL mutants and the oxidative-stress-dependent formation of mixed disulfides between YajL and members of the thiol proteome. We report here that yajL mutants display increased protein sulfenic acids levels and that formation of mixed disulfides between YajL and its protein substrates in vivo is inhibited by the sulfenic acid reactant dimedone, suggesting that YajL preferentially forms disulfides with sulfenylated proteins. YajL (but not YajL(C106A)) also forms mixed disulfides in vitro with the sulfenylated form of bovine serum albumin. The YajL-serum albumin disulfides can be subsequently reduced by glutathione or dihydrolipoic acid. We also show that DJ-1 can form mixed disulfides with sulfenylated E. coli proteins and with sulfenylated serum albumin. These results suggest that YajL and possibly DJ-1 function as covalent chaperones involved in the detection of sulfenylated proteins by forming mixed disulfides with them and that these disulfides are subsequently reduced by low-molecular-weight thiols. |
| Databáze: | OpenAIRE |
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