4.5 Article

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

期刊

FEBS LETTERS
卷 588, 期 23, 页码 4342-4347

出版社

WILEY
DOI: 10.1016/j.febslet.2014.09.044

关键词

Chloroplast NADPH-dependent thioredoxin-reductase; NTRC; Thioredoxin; Peroxiredoxin; Molecular recognition; Isothermal titration calorimetry; Bimolecular fluorescence complementation

资金

  1. Andalusian Government [BIO-182, CVI-5919]
  2. ERDF [BIO-022, CVI-4528]
  3. Ministry of Science and Innovation [BIO2010-15430, BFU2010-19451]
  4. Spanish Ministry of Economy and Competitiveness

向作者/读者索取更多资源

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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