Overexpression of Arabidopsis NADPH-dependent thioredoxin reductase C (AtNTRC) confers freezing and cold shock tolerance to plants
- Authors
- Moon, Jeong Chan; Lee, Sangmin; Shin, Su Young; Chae, Ho Byoung; Jung, Young Jun; Jung, Hyun Suk; Lee, Kyun Oh; Lee, Jung Ro; Lee, Sang Yeol
- Issue Date
- 7-Aug-2015
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- NADPH-dependent thioredoxin reductase; DNA binding; Thioredoxin; Peroxiredoxin; Cryoprotective activity
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.463, no.4, pp 1225 - 1229
- Pages
- 5
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 463
- Number
- 4
- Start Page
- 1225
- End Page
- 1229
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/17080
- DOI
- 10.1016/j.bbrc.2015.06.089
- ISSN
- 0006-291X
1090-2104
- Abstract
- Overexpression of AtNTRC (AtNTRCOE) in Arabidopsis thaliana led to a freezing and cold stress tolerance, whereas a knockout mutant (atntrc) showed a stress-sensitive phenotype. Biochemical analyses showed that the recombinant AtNTRC proteins exhibited a cryoprotective activity for malate dehydrogenase and lactic dehydrogenase. Furthermore, conclusive evidence of its interaction with nucleic acids in vitro is provided here on the basis of gel shift and electron microscopy analysis. Recombinant AtNTRC efficiently protected RNA and DNA from RNase A and metal catalyzed oxidation damage, respectively. The C-terminal thioredoxin domain is required for the nucleic acid-protein complex formation. From these results, it can be hypothesized that AtNTRC, which is known to be an electron donor of peroxiredoxin, contributes the stability of macromolecules under cold stress. (C) 2015 Elsevier Inc. All rights reserved.
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