Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions
2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces...
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todo:paper_1742464X_v276_n9_p2478_Aran2023-10-03T16:30:20Z Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions Aran, M. Ferrero, D.S. Pagano, E. Wolosiuk, R.A. 2-Cys peroxiredoxin ATP binding Autophosphorylation Molecular chaperone Oligomerization Overoxidation Oxidative stress Peroxidase mechanism Sulfenic acid Sulfinic-phosphoryl anhydride cysteine disulfide peroxidase peroxide peroxiredoxin thiol acetylation covalent bond molecular interaction molecular model nonhuman oligomerization oxidation oxidative stress priority journal protein phosphorylation protein processing protein quaternary structure protein targeting proteomics regulatory mechanism review signal transduction Animals Cysteine Humans Molecular Chaperones Oxidation-Reduction Oxidative Stress Peroxidases Peroxiredoxins Phosphorylation Protein Processing, Post-Translational Sulfenic Acids 2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces not only the usual thiol-disulfide exchange but also higher oxidation states of the sulfur atom. These changes are part of a complex system wherein the cooperation with other post-translational modifications - phosphorylation, acetylation - may function as major regulatory mechanisms of the quaternary structure. More importantly, modern proteomic approaches have identified the oxyacids at cysteine residues as novel protein targets for unsuspected post-translational modifications, such as phosphorylation that yields the unusual sulfi(o)nic-phosphoryl anhydride. In this article, we review the biochemical attributes of 2-Cys peroxiredoxins that, in combination with complementary studies of forward and reverse genetics, have generated stimulating molecular models to explain how this enzyme integrates into cell signaling in vivo. © 2009 FEBS. Fil:Aran, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pagano, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wolosiuk, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
2-Cys peroxiredoxin ATP binding Autophosphorylation Molecular chaperone Oligomerization Overoxidation Oxidative stress Peroxidase mechanism Sulfenic acid Sulfinic-phosphoryl anhydride cysteine disulfide peroxidase peroxide peroxiredoxin thiol acetylation covalent bond molecular interaction molecular model nonhuman oligomerization oxidation oxidative stress priority journal protein phosphorylation protein processing protein quaternary structure protein targeting proteomics regulatory mechanism review signal transduction Animals Cysteine Humans Molecular Chaperones Oxidation-Reduction Oxidative Stress Peroxidases Peroxiredoxins Phosphorylation Protein Processing, Post-Translational Sulfenic Acids |
| spellingShingle |
2-Cys peroxiredoxin ATP binding Autophosphorylation Molecular chaperone Oligomerization Overoxidation Oxidative stress Peroxidase mechanism Sulfenic acid Sulfinic-phosphoryl anhydride cysteine disulfide peroxidase peroxide peroxiredoxin thiol acetylation covalent bond molecular interaction molecular model nonhuman oligomerization oxidation oxidative stress priority journal protein phosphorylation protein processing protein quaternary structure protein targeting proteomics regulatory mechanism review signal transduction Animals Cysteine Humans Molecular Chaperones Oxidation-Reduction Oxidative Stress Peroxidases Peroxiredoxins Phosphorylation Protein Processing, Post-Translational Sulfenic Acids Aran, M. Ferrero, D.S. Pagano, E. Wolosiuk, R.A. Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| topic_facet |
2-Cys peroxiredoxin ATP binding Autophosphorylation Molecular chaperone Oligomerization Overoxidation Oxidative stress Peroxidase mechanism Sulfenic acid Sulfinic-phosphoryl anhydride cysteine disulfide peroxidase peroxide peroxiredoxin thiol acetylation covalent bond molecular interaction molecular model nonhuman oligomerization oxidation oxidative stress priority journal protein phosphorylation protein processing protein quaternary structure protein targeting proteomics regulatory mechanism review signal transduction Animals Cysteine Humans Molecular Chaperones Oxidation-Reduction Oxidative Stress Peroxidases Peroxiredoxins Phosphorylation Protein Processing, Post-Translational Sulfenic Acids |
| description |
2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces not only the usual thiol-disulfide exchange but also higher oxidation states of the sulfur atom. These changes are part of a complex system wherein the cooperation with other post-translational modifications - phosphorylation, acetylation - may function as major regulatory mechanisms of the quaternary structure. More importantly, modern proteomic approaches have identified the oxyacids at cysteine residues as novel protein targets for unsuspected post-translational modifications, such as phosphorylation that yields the unusual sulfi(o)nic-phosphoryl anhydride. In this article, we review the biochemical attributes of 2-Cys peroxiredoxins that, in combination with complementary studies of forward and reverse genetics, have generated stimulating molecular models to explain how this enzyme integrates into cell signaling in vivo. © 2009 FEBS. |
| format |
JOUR |
| author |
Aran, M. Ferrero, D.S. Pagano, E. Wolosiuk, R.A. |
| author_facet |
Aran, M. Ferrero, D.S. Pagano, E. Wolosiuk, R.A. |
| author_sort |
Aran, M. |
| title |
Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| title_short |
Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| title_full |
Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| title_fullStr |
Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| title_full_unstemmed |
Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| title_sort |
typical 2-cys peroxiredoxins - modulation by covalent transformations and noncovalent interactions |
| url |
http://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran |
| work_keys_str_mv |
AT aranm typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions AT ferrerods typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions AT paganoe typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions AT wolosiukra typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions |
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1782025465735675904 |