Artículo
Molecular recognition in the interaction of chloroplast 2-Cys peroxiredoxin with NADPH-thioredoxin reductase C (NTRC) and thioredoxin x
Autor/es | Bernal Bayard, Pilar
Ojeda Servián, Valle Hervás Morón, Manuel Cejudo Fernández, Francisco Javier Navarro Carruesco, José Antonio Velázquez Campoy, Adrián Pérez Ruiz, Juan Manuel |
Departamento | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Fecha de publicación | 2014 |
Fecha de depósito | 2018-01-18 |
Publicado en |
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Resumen | 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). ... 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. |
Agencias financiadoras | Junta de Andalucía Ministerio de Ciencia e Innovación (MICIN). España |
Identificador del proyecto | BIO-022
CVI-4528 BIO-182 CVI-5919 BIO2010-15430 BFU2010-19451 |
Cita | Bernal Bayard, P., Ojeda Servián, 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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