| Literature DB >> 26086110 |
Jeong Chan Moon1, Sangmin Lee2, Su Young Shin1, Ho Byoung Chae3, Young Jun Jung3, Hyun Suk Jung2, Kyun Oh Lee3, Jung Ro Lee4, Sang Yeol Lee5.
Abstract
Overexpression of AtNTRC (AtNTRC(OE)) 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.Entities:
Keywords: Cryoprotective activity; DNA binding; NADPH-dependent thioredoxin reductase; Peroxiredoxin; Thioredoxin
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Year: 2015 PMID: 26086110 DOI: 10.1016/j.bbrc.2015.06.089
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575