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Molecular recognition in the interaction of chloroplast 2‐Cys peroxiredoxin with NADPH‐thioredoxin reductase C (NTRC) and thioredoxin x
Author(s) -
Bernal-Bayard Pilar,
Ojeda Valle,
Hervás Manuel,
Cejudo Francisco J.,
Navarro José A.,
Velázquez-Campoy Adrián,
Pérez-Ruiz Juan M.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.044
Subject(s) - ferredoxin thioredoxin reductase , thioredoxin , peroxiredoxin , thioredoxin reductase , bimolecular fluorescence complementation , biochemistry , chemistry , chloroplast , biology , enzyme , gene , peroxidase
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 .