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Molecular recognition in the interaction of chloroplast 2-Cys peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin x

 

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Opened Access Molecular recognition in the interaction of chloroplast 2-Cys peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin x
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Author: Bernal Bayard, Pilar
Ojeda, Valle
Hervás Morón, Manuel
Cejudo Fernández, Francisco Javier
Navarro Carruesco, José Antonio
Velázquez Campoy, Adrián
Pérez Ruiz, Juan Manuel
Department: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Date: 2014
Published in: FEBS Letters, 588 (23), 4342-4347.
Document type: Article
Abstract: In addition to the standard NADPH thioredoxin reductases (NTRs), plants hold a plastidic NTR (NTRC), with a thioredoxin module fused at the C-terminus. NTRC is an efficient reductant of 2-Cys peroxiredoxins (2-Cys Prxs). The interaction of NTRC and chloroplastic thioredoxin x with 2-Cys Prxs has been confirmed in vivo, by bimolecular fluorescence complementation (BiFC) assays, and in vitro, by isothermal titration calorimetry (ITC) experiments. In comparison with thioredoxin x, NTRC interacts with 2-Cys Prx with higher affinity, both the thioredoxin and NTR domains of NTRC contributing significantly to this interaction, as demonstrated by using the NTR and thioredoxin modules of the enzyme expressed separately. The presence of the thioredoxin domain seems to prevent the interaction of NTRC with thioredoxin x.
Cite: Bernal Bayard, P., Ojeda, V., Hervás Morón, M., Cejudo Fernández, F.J., Navarro Carruesco, J.A., Velázquez Campoy, A. y Pérez Ruiz, J.M. (2014). Molecular recognition in the interaction of chloroplast 2-Cys peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin x. FEBS Letters, 588 (23), 4342-4347.
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URI: https://hdl.handle.net/11441/69192

DOI: 10.1016/j.febslet.2014.09.044

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