Evidence that thiol-based redox state is critical for xylem vessel cell differentiation.

Nitric oxide (NO), which plays essential roles in a variety of cell signaling processes, is the precursor of a family of NO-derived molecules, including toxic reactive nitrogen species. The NO-based regulation of cellular activity is mediated by the reversible modification of cysteine thiol groups in redox-sensitive proteins. One such modification is protein S-nitrosylation, i.e., the addition of an NO moiety to a cysteine thiol, and this S-nitrosylation is regulated by enzymes such as S-nitrosoglutathione reductase (GSNOR). Recently, we reported a novel loss-of-function allele of gsnor1, named suppressor of ectopic vessel cell differentiation induced by VND7-1 (seiv1), based on the VND7-inducible system, in which almost all cell types are transdifferentiated into xylem vessel cells upon activation of the NAC transcription factor VND7. We also found that VND7 can be S-nitrosylated and that the target cysteine residues for S-nitrosylation are critical for VND7 transactivation activity. Here, we further discuss roles for GSNOR1 in xylem vessel cell differentiation, and provide additional data on the effects of cellular NO level on VND7 activity.