ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin
2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous peroxidases with important roles in cellular antioxidant defense and hydrogen peroxide-mediated signaling. Post-translational modifications of conserved cysteines cause the transition from low to high molecular weight oligomers, triggering the functio...
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2011
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v286_n26_p23441_Aran http://hdl.handle.net/20.500.12110/paper_00219258_v286_n26_p23441_Aran |
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paper:paper_00219258_v286_n26_p23441_Aran |
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record_format |
dspace |
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 ,2 ,2-trifluoroethanol Antioxidant defense Chaperone activity Conserved residues Cosolvents Cysteine residues Decamers Functional changes Helical conformation Higher order In-line Low-to-high Molecular chaperones Native conformation Non-covalent interaction Peroxiredoxins Post-translational modifications Quaternary structure Redox transformations Self-polymerization Amino acids Chlorophyll Conformations Dichroism Ethanol Hydrogen peroxide Oligomerization Polymerization Spheres Transmission electron microscopy Oligomers 2 cysteine peroxiredoxin adenosine triphosphate arginine cysteine magnesium ion peroxiredoxin trifluoroethanol unclassified drug magnesium peroxiredoxin recombinant protein vegetable protein alpha helix article beta sheet cell energy chloroplast circular dichroism controlled study enzyme activity enzyme regulation molecular interaction molecular weight nonhuman oligomerization oxidation reduction reaction particle size photochemistry priority journal protein aggregation protein analysis protein conformation protein function protein polymerization protein processing protein quaternary structure rapeseed surface plasmon resonance transmission electron microscopy chemistry chloroplast enzymology genetics metabolism protein multimerization protein secondary structure Adenosine Triphosphate Chloroplasts Circular Dichroism Magnesium Peroxiredoxins Plant Proteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Recombinant Proteins |
spellingShingle |
2 ,2 ,2-trifluoroethanol Antioxidant defense Chaperone activity Conserved residues Cosolvents Cysteine residues Decamers Functional changes Helical conformation Higher order In-line Low-to-high Molecular chaperones Native conformation Non-covalent interaction Peroxiredoxins Post-translational modifications Quaternary structure Redox transformations Self-polymerization Amino acids Chlorophyll Conformations Dichroism Ethanol Hydrogen peroxide Oligomerization Polymerization Spheres Transmission electron microscopy Oligomers 2 cysteine peroxiredoxin adenosine triphosphate arginine cysteine magnesium ion peroxiredoxin trifluoroethanol unclassified drug magnesium peroxiredoxin recombinant protein vegetable protein alpha helix article beta sheet cell energy chloroplast circular dichroism controlled study enzyme activity enzyme regulation molecular interaction molecular weight nonhuman oligomerization oxidation reduction reaction particle size photochemistry priority journal protein aggregation protein analysis protein conformation protein function protein polymerization protein processing protein quaternary structure rapeseed surface plasmon resonance transmission electron microscopy chemistry chloroplast enzymology genetics metabolism protein multimerization protein secondary structure Adenosine Triphosphate Chloroplasts Circular Dichroism Magnesium Peroxiredoxins Plant Proteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Recombinant Proteins Arán, Martín Mora García, Santiago Wolosiuk, Ricardo Alejandro ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
topic_facet |
2 ,2 ,2-trifluoroethanol Antioxidant defense Chaperone activity Conserved residues Cosolvents Cysteine residues Decamers Functional changes Helical conformation Higher order In-line Low-to-high Molecular chaperones Native conformation Non-covalent interaction Peroxiredoxins Post-translational modifications Quaternary structure Redox transformations Self-polymerization Amino acids Chlorophyll Conformations Dichroism Ethanol Hydrogen peroxide Oligomerization Polymerization Spheres Transmission electron microscopy Oligomers 2 cysteine peroxiredoxin adenosine triphosphate arginine cysteine magnesium ion peroxiredoxin trifluoroethanol unclassified drug magnesium peroxiredoxin recombinant protein vegetable protein alpha helix article beta sheet cell energy chloroplast circular dichroism controlled study enzyme activity enzyme regulation molecular interaction molecular weight nonhuman oligomerization oxidation reduction reaction particle size photochemistry priority journal protein aggregation protein analysis protein conformation protein function protein polymerization protein processing protein quaternary structure rapeseed surface plasmon resonance transmission electron microscopy chemistry chloroplast enzymology genetics metabolism protein multimerization protein secondary structure Adenosine Triphosphate Chloroplasts Circular Dichroism Magnesium Peroxiredoxins Plant Proteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Recombinant Proteins |
description |
2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous peroxidases with important roles in cellular antioxidant defense and hydrogen peroxide-mediated signaling. Post-translational modifications of conserved cysteines cause the transition from low to high molecular weight oligomers, triggering the functional change from peroxidase to molecular chaperone. However, it remains unclear how non-covalent interactions of 2-Cys Prx with metabolites modulate the quaternary structure. Here, we disclose that ATP and Mg2+ (ATP/Mg) promote the self-polymerization of chloroplast 2-Cys Prx (polypeptide 23.5 kDa) into soluble higher order assemblies (>2 MDa) that proceed to insoluble aggregates beyond 5mMATP. Remarkably, the withdrawal of ATP or Mg2+ brings soluble oligomers and insoluble aggregates back to the native conformation without compromising the associated functions. As confirmed by transmission electron microscopy, ATP/Mg drive the toroid-like decamers (diameter 13 nm) to the formation of large sphere-like particles (diameter ∼30 nm). Circular dichroism studies on ATP-labeled 2-Cys Prx reveal that ATP/Mg enhance the proportion of β-sheets with the concurrent decrease in the content of α-helices. In line with this observation, the formation of insoluble aggregates is strongly prevented by 2,2,2-trifluoroethanol, a cosolvent employed to induce α-helical conformations. We further find that the response of self-polymerization to ATP/Mg departs abruptly from that of the associated peroxidase and chaperone activities when two highly conserved residues, Arg129 and Arg152, are mutated. Collectively, our data uncover that non-covalent interactions of ATP/Mg with 2-Cys Prx modulate dynamically the quaternary structure, thereby coupling the non-redox chemistry of cell energy with redox transformations at cysteine residues. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. |
author |
Arán, Martín Mora García, Santiago Wolosiuk, Ricardo Alejandro |
author_facet |
Arán, Martín Mora García, Santiago Wolosiuk, Ricardo Alejandro |
author_sort |
Arán, Martín |
title |
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
title_short |
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
title_full |
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
title_fullStr |
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
title_full_unstemmed |
ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin |
title_sort |
atp and mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-cys peroxiredoxin |
publishDate |
2011 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v286_n26_p23441_Aran http://hdl.handle.net/20.500.12110/paper_00219258_v286_n26_p23441_Aran |
work_keys_str_mv |
AT aranmartin atpandmg2promotethereversibleoligomerizationandaggregationofchloroplast2cysperoxiredoxin AT moragarciasantiago atpandmg2promotethereversibleoligomerizationandaggregationofchloroplast2cysperoxiredoxin AT wolosiukricardoalejandro atpandmg2promotethereversibleoligomerizationandaggregationofchloroplast2cysperoxiredoxin |
_version_ |
1768545678986838016 |
spelling |
paper:paper_00219258_v286_n26_p23441_Aran2023-06-08T14:43:31Z ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin Arán, Martín Mora García, Santiago Wolosiuk, Ricardo Alejandro 2 ,2 ,2-trifluoroethanol Antioxidant defense Chaperone activity Conserved residues Cosolvents Cysteine residues Decamers Functional changes Helical conformation Higher order In-line Low-to-high Molecular chaperones Native conformation Non-covalent interaction Peroxiredoxins Post-translational modifications Quaternary structure Redox transformations Self-polymerization Amino acids Chlorophyll Conformations Dichroism Ethanol Hydrogen peroxide Oligomerization Polymerization Spheres Transmission electron microscopy Oligomers 2 cysteine peroxiredoxin adenosine triphosphate arginine cysteine magnesium ion peroxiredoxin trifluoroethanol unclassified drug magnesium peroxiredoxin recombinant protein vegetable protein alpha helix article beta sheet cell energy chloroplast circular dichroism controlled study enzyme activity enzyme regulation molecular interaction molecular weight nonhuman oligomerization oxidation reduction reaction particle size photochemistry priority journal protein aggregation protein analysis protein conformation protein function protein polymerization protein processing protein quaternary structure rapeseed surface plasmon resonance transmission electron microscopy chemistry chloroplast enzymology genetics metabolism protein multimerization protein secondary structure Adenosine Triphosphate Chloroplasts Circular Dichroism Magnesium Peroxiredoxins Plant Proteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Recombinant Proteins 2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous peroxidases with important roles in cellular antioxidant defense and hydrogen peroxide-mediated signaling. Post-translational modifications of conserved cysteines cause the transition from low to high molecular weight oligomers, triggering the functional change from peroxidase to molecular chaperone. However, it remains unclear how non-covalent interactions of 2-Cys Prx with metabolites modulate the quaternary structure. Here, we disclose that ATP and Mg2+ (ATP/Mg) promote the self-polymerization of chloroplast 2-Cys Prx (polypeptide 23.5 kDa) into soluble higher order assemblies (>2 MDa) that proceed to insoluble aggregates beyond 5mMATP. Remarkably, the withdrawal of ATP or Mg2+ brings soluble oligomers and insoluble aggregates back to the native conformation without compromising the associated functions. As confirmed by transmission electron microscopy, ATP/Mg drive the toroid-like decamers (diameter 13 nm) to the formation of large sphere-like particles (diameter ∼30 nm). Circular dichroism studies on ATP-labeled 2-Cys Prx reveal that ATP/Mg enhance the proportion of β-sheets with the concurrent decrease in the content of α-helices. In line with this observation, the formation of insoluble aggregates is strongly prevented by 2,2,2-trifluoroethanol, a cosolvent employed to induce α-helical conformations. We further find that the response of self-polymerization to ATP/Mg departs abruptly from that of the associated peroxidase and chaperone activities when two highly conserved residues, Arg129 and Arg152, are mutated. Collectively, our data uncover that non-covalent interactions of ATP/Mg with 2-Cys Prx modulate dynamically the quaternary structure, thereby coupling the non-redox chemistry of cell energy with redox transformations at cysteine residues. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Fil:Aran, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mora-García, S. 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. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v286_n26_p23441_Aran http://hdl.handle.net/20.500.12110/paper_00219258_v286_n26_p23441_Aran |