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Redox-dependent structural switch and CBF activation confer freezing tolerance in plants.

Eun Seon LeeJoung Hun ParkSeong Dong WiChang Ho KangYong Hun ChiHo Byoung ChaeSeol Ki PaengMyung Geun JiWoe Yeon KimMin Gab KimDae-Jin YunGary StaceySang Yeol Lee
Published in: Nature plants (2021)
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.
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