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
- 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
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据