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In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.
Redox Biol. 2015 Dec; 6:326-333.RB

Abstract

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.

Authors+Show Affiliations

Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France.Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France.Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France.Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France.Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France.Department of Chemistry and Molecular Biology (CMB), University of Gothenburg, Medicinaregatan 9C, S-413 90 Göteborg, Sweden.Department of Chemistry and Molecular Biology (CMB), University of Gothenburg, Medicinaregatan 9C, S-413 90 Göteborg, Sweden.Oxidative Stress and Cancer, IBITECS, SBIGEM, CEA-Saclay, 91191 Gif-sur-Yvette, France. Electronic address: Michel.toledano@cea.fr.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

26335398

Citation

Noichri, Y, et al. "In Vivo Parameters Influencing 2-Cys Prx Oligomerization: the Role of Enzyme Sulfinylation." Redox Biology, vol. 6, 2015, pp. 326-333.
Noichri Y, Palais G, Ruby V, et al. In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation. Redox Biol. 2015;6:326-333.
Noichri, Y., Palais, G., Ruby, V., D'Autreaux, B., Delaunay-Moisan, A., Nyström, T., Molin, M., & Toledano, M. B. (2015). In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation. Redox Biology, 6, 326-333. https://doi.org/10.1016/j.redox.2015.08.011
Noichri Y, et al. In Vivo Parameters Influencing 2-Cys Prx Oligomerization: the Role of Enzyme Sulfinylation. Redox Biol. 2015;6:326-333. PubMed PMID: 26335398.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation. AU - Noichri,Y, AU - Palais,G, AU - Ruby,V, AU - D'Autreaux,B, AU - Delaunay-Moisan,A, AU - Nyström,T, AU - Molin,M, AU - Toledano,M B, Y1 - 2015/08/20/ PY - 2015/06/25/received PY - 2015/08/10/revised PY - 2015/08/11/accepted PY - 2015/9/4/entrez PY - 2015/9/4/pubmed PY - 2016/9/3/medline KW - Chaperone KW - H(2)O(2) KW - Peroxidase KW - Peroxiredoxin KW - S. cerevisiae KW - Sulfiredoxin SP - 326 EP - 333 JF - Redox biology JO - Redox Biol VL - 6 N2 - 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. SN - 2213-2317 UR - https://www.unboundmedicine.com/medline/citation/26335398/In_vivo_parameters_influencing_2_Cys_Prx_oligomerization:_The_role_of_enzyme_sulfinylation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S2213-2317(15)00101-9 DB - PRIME DP - Unbound Medicine ER -