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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Detalles Bibliográficos
Autores principales:	Arán, Martín, Pagano, Eleonora, Wolosiuk, Ricardo Alejandro
Publicado:	2009
Materias:	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
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v276_n9_p2478_Aran http://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_1742464X_v276_n9_p2478_Aran
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spelling	paper:paper_1742464X_v276_n9_p2478_Aran2023-06-08T16:27:03Z Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions Arán, Martín Pagano, Eleonora Wolosiuk, Ricardo Alejandro 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. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v276_n9_p2478_Aran http://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	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 Arán, Martín Pagano, Eleonora Wolosiuk, Ricardo Alejandro 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.
author	Arán, Martín Pagano, Eleonora Wolosiuk, Ricardo Alejandro
author_facet	Arán, Martín Pagano, Eleonora Wolosiuk, Ricardo Alejandro
author_sort	Arán, Martín
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
publishDate	2009
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v276_n9_p2478_Aran http://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran
work_keys_str_mv	AT aranmartin typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions AT paganoeleonora typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions AT wolosiukricardoalejandro typical2cysperoxiredoxinsmodulationbycovalenttransformationsandnoncovalentinteractions
_version_	1768543153129783296

Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions

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