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Título

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

Autor Bernal-Bayard, P. ; Ojeda, Valle; Hervás, Manuel ; Cejudo, Francisco Javier ; Navarro, José A. ; Velázquez-Campoy, Adrián; Pérez-Ruiz, Juan Manuel
Fecha de publicación 2014
EditorElsevier
Citación FEBS Letters, 588(23): 4342-4347 (2014)
ResumenIn 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.
Versión del editorhttp://dx.doi.org/10.1016/j.febslet.2014.09.044
URI http://hdl.handle.net/10261/108483
DOI10.1016/j.febslet.2014.09.044
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