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Author 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
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword APPLIED LIFE SCIENCES ♦ AGGLOMERATION ♦ ARABIDOPSIS ♦ DNA ♦ ELECTRON MICROSCOPY ♦ FREEZING ♦ GELS ♦ IN VITRO ♦ METALS ♦ OXIDATION ♦ PHENOTYPE ♦ PROTEINS ♦ RNA ♦ STRESSES ♦ VALENCE
Abstract Overexpression of AtNTRC (AtNTRC{sup 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. - Highlights: • AtNTRC has a cryoprotective activity in vitro. • Overexpression of AtNTRC increases tolerance to freezing and cold shock stresses. • Thioredoxin domain of AtNTRC protects nucleic acids in vitro. • AtNTRC inhibits protein aggregation under freezing stress in vitro.
ISSN 0006291X
Educational Use Research
Learning Resource Type Article
Publisher Date 2015-08-07
Publisher Place United States
Journal Biochemical and Biophysical Research Communications
Volume Number 463
Issue Number 4


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