1. Redox-dependent structural switch and CBF activation confer freezing tolerance in plants
- Author
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Myung Geun Ji, Chang Ho Kang, Gary Stacey, Sang Yeol Lee, Joung Hun Park, Ho Byoung Chae, Woe-Yeon Kim, Seong Dong Wi, Yong Hun Chi, Eun Seon Lee, Min Gab Kim, Seol Ki Paeng, and Dae-Jin Yun
- Subjects
animal structures ,biology ,Chemistry ,Plant Science ,biology.organism_classification ,Cell biology ,Cytosol ,Cytoplasm ,Arabidopsis ,Glycine ,Gene expression ,Thioredoxin ,Transcription factor ,Myristoylation - Abstract
The activities of cold-responsive C-repeat-binding transcription factors (CBFs) are tightly controlled as they not only induce cold tolerance but also regulate normal plant growth under temperate conditions1-4. Thioredoxin h2 (Trx-h2)-a cytosolic redox protein identified as an interacting partner of CBF1-is normally anchored to cytoplasmic endomembranes through myristoylation at the second glycine residue5,6. However, after exposure to cold conditions, the demyristoylated Trx-h2 is translocated to the nucleus, where it reduces the oxidized (inactive) CBF oligomers and monomers. The reduced (active) monomers activate cold-regulated gene expression. Thus, in contrast to the Arabidopsis trx-h2 (AT5G39950) null mutant, Trx-h2 overexpression lines are highly cold tolerant. Our findings reveal the mechanism by which cold-mediated redox changes induce the structural switching and functional activation of CBFs, therefore conferring plant cold tolerance.
- Published
- 2021
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