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

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 conditions 1 – 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 residue 5 , 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.