In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation
| Autor: | Benoît D'Autréaux, V. Ruby, Gael Palais, Y. Noichri, Mikael Molin, Agnès Delaunay-Moisan, Thomas Nyström, Michel B. Toledano |
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| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Stress Oxydatif et Cancer (SOC), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2015 |
| Předmět: |
[SDV]Life Sciences [q-bio]
H2O2 Clinical Biochemistry Mutant S. cerevisiae Chaperone Biochemistry Gene Expression Regulation Fungal chemistry.chemical_classification 0303 health sciences Chromatography Gel biology 030302 biochemistry & molecular biology Peroxiredoxin 3. Good health Isoenzymes Fungal Peroxidases Chromatography Gel Peroxidase Research Paper Plasmids Protein Structure Saccharomyces cerevisiae Proteins Recombinant Fusion Proteins Saccharomyces cerevisiae Quaternary 03 medical and health sciences Protein Structure Quaternary 030304 developmental biology Organic Chemistry Wild type H(2)O(2) Hydrogen Peroxide Sulfinic Acids Sulfiredoxin Enzyme chemistry Gene Expression Regulation Chaperone (protein) Mutation biology.protein Protein quaternary structure Protein Multimerization Molecular Chaperones |
| Zdroj: | Redox Biology Redox Biology, 2015, 6, pp.326--333. ⟨10.1016/j.redox.2015.08.011⟩ |
| ISSN: | 2213-2317 |
| DOI: | 10.1016/j.redox.2015.08.011 |
| Popis: | 2-Cys Prxs are H2O2-specific antioxidants that become inactivated by enzyme hyperoxidation at elevated H2O2 levels. Although hyperoxidation restricts the antioxidant physiological role of these enzymes, it also allows the enzyme to become an efficient chaperone holdase. The critical molecular event allowing the peroxidase to chaperone switch is thought to be the enzyme assembly into high molecular weight (HMW) structures brought about by enzyme hyperoxidation. How hyperoxidation promotes HMW assembly is not well understood and Prx mutants allowing disentangling its peroxidase and chaperone functions are lacking. To begin addressing the link between enzyme hyperoxidation and HMW structures formation, we have evaluated the in vivo 2-Cys Prxs quaternary structure changes induced by H2O2 by size exclusion chromatography (SEC) on crude lysates, using wild type (Wt) untagged and Myc-tagged S. cerevisiae 2-Cys Prx Tsa1 and derivative Tsa1 mutants or genetic conditions known to inactivate peroxidase or chaperone activity or altering the enzyme sensitivity to hyperoxidation. Our data confirm the strict causative link between H2O2-induced hyperoxidation and HMW formation/stabilization, also raising the question of whether CP hyperoxidation triggers the assembly of HMW structures by the stacking of decamers, which is the prevalent view of the literature, or rather, the stabilization of preassembled stacked decamers. Graphical abstract |
| Databáze: | OpenAIRE |
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