Journal
FEBS LETTERS
Volume 588, Issue 23, Pages 4342-4347Publisher
WILEY
DOI: 10.1016/j.febslet.2014.09.044
Keywords
Chloroplast NADPH-dependent thioredoxin-reductase; NTRC; Thioredoxin; Peroxiredoxin; Molecular recognition; Isothermal titration calorimetry; Bimolecular fluorescence complementation
Funding
- Andalusian Government [BIO-182, CVI-5919]
- ERDF [BIO-022, CVI-4528]
- Ministry of Science and Innovation [BIO2010-15430, BFU2010-19451]
- Spanish Ministry of Economy and Competitiveness
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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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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