ArticleJournal of experimental botany2013
The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.
Article in Journal of experimental botany, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 94 citations in OpenAlex.
- The interactome of the Bakers' yeast peroxiredoxin Tsa1 implicates it in redox regulation of intermediary metabolism, glycolysis, and zinc homeostasis.Metallomics : integrated biometal science · 2025Article
- 2-Cys peroxiredoxins contribute to thylakoid lipid unsaturation by affecting ω-3 fatty acid desaturase 8.Plant physiology · 2024Article
- Novel insight into functions of ascorbate peroxidase in higher plants: More than a simple antioxidant enzyme.Redox biology · 2023Review
- Sulfiredoxin Promotes Cancer Cell Invasion through Regulation of the miR143-Fascin Axis.Molecular and cellular biology · 2022Article
- Protein-protein interactions in plant antioxidant defense.Frontiers in plant science · 2022Review
- Role of the Filifactor alocis Hypothetical Protein FA519 in Oxidative Stress Resistance.Microbiology spectrum · 2021Article
- Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins.iScience · 2021Article
- The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation.Antioxidants (Basel, Switzerland) · 2021Article
- Function and Regulation of Chloroplast Peroxiredoxin IIE.Antioxidants (Basel, Switzerland) · 2021Article
- Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.Antioxidants (Basel, Switzerland) · 2020Article
- A Peroxiredoxin From theFrontiers in cellular and infection microbiology · 2020Article
- A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target inFrontiers in veterinary science · 2020Article
- Aromatic Residues at the Dimer-Dimer Interface in the Peroxiredoxin Tsa1 Facilitate Decamer Formation and Biological Function.Chemical research in toxicology · 2019Article
- Piecing Together How Peroxiredoxins Maintain Genomic Stability.Antioxidants (Basel, Switzerland) · 2018Review
- Article
- Crystal structure of Arabidopsis thaliana peroxiredoxin A C119S mutant.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone.Scientific reports · 2018Article
- Suppression of External NADPH Dehydrogenase-NDB1 inInternational journal of molecular sciences · 2018Article
- Peroxiredoxins and Redox Signaling in Plants.Antioxidants & redox signaling · 2018Review
- Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Antioxidants & redox signaling · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
2-Cysteine peroxiredoxins (2-CysPrxs) are ubiquitous and highly abundant proteins that serve multiple functions as peroxidases, chaperones, and thiol oxidases and in redox-dependent cell signalling. The chloroplast protein plays a role in seedling development and protection of the photosynthetic apparatus. This study aimed to unequivocally link conformation and function. To this end, a set of non-tagged site-directed mutagenized At2-CysPrx variants was engineered, which mimicked the conformational states and their specific functions: hyperoxidized form (C54D), reduced form (C54S, C176S), oxidized form (C54DC176K), phosphorylated form (T92D), reduced ability for oligomerization by interfering with the dimer-dimer interface (F84R) and a C-terminally truncated form [ΔC (-20 aa)]. These variants were fully or partly fixed in their quaternary structure and function, respectively, and were analysed for their conformational state and peroxidase and chaperone activity, as well as for their sensitivity to hyperoxidation. The presence of a His6-tag strongly influenced the properties of the protein. The ΔC variant became insensitive to hyperoxidation, while T92D and F84R became more sensitive. The C54D variant revealed the highest chaperone activity. The highest peroxidase activity was observed for the F84R and ΔC variants. Efficient interaction with NADP-dependent thioredoxin reductase C depended on the presence of Cys residues and the C-terminal tail. The results suggest that the structural flexibility is important for the switch between peroxidase and chaperone function and that evolution has conserved the functional switch instead of maximizing a single function. These variants are ideal tools for future conformation-specific studies in vivo and in vitro.
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