Protein S-Nitrosylation Regulates Xylem Vessel Cell Differentiation in Arabidopsis. (13th October 2017)

• Record Type: Journal Article
• Authors: Kawabe, Harunori; Ohtani, Misato; Kurata, Tetsuya; Sakamoto, Tomoaki; Demura, Taku
• Is Part Of: Plant & cell physiology. Volume 59:Number 1(2018)
• Page Start: 17
• Page End: 29
• Publication Date: 2017-10-13
• Subjects: GSNOR1 -- S-nitrosylation -- seiv mutant -- Transcription factor -- VND7 -- Xylem vessel cell differentiation; Plant physiology -- Periodicals; Microbiology -- Periodicals; Cytology -- Periodicals; Cell Physiology -- Periodicals; Plant Physiological Phenomena -- Periodicals; Cytology; Microbiology; Plant physiology; Periodicals; 571.205
• DOI: 10.1093/pcp/pcx151
• Languages: English
• ISSNs: 0032-0781

Abstract

Abstract: Post-translational modifications of proteins have important roles in the regulation of protein activity. One such modification, S -nitrosylation, involves the covalent binding of nitric oxide (NO)-related species to a cysteine residue. Recent work showed that protein S -nitrosylation has crucial functions in plant development and environmental responses. In the present study, we investigated the importance of protein S -nitrosylation for xylem vessel cell differentiation using a forward genetics approach. We performed ethyl methanesulfonate mutagenesis of a transgenic Arabidopsis 35S::VND7-VP16-GR line in which the activity of VASCULAR-RELATED NAC-DOMAIN7 (VND7), a key transcription factor involved in xylem vessel cell differentiation, can be induced post-translationally by glucocorticoid treatment, with the goal of obtaining suppressor mutants that failed to differentiate ectopic xylem vessel cells; we named these mutants suppressor of ectopic vessel cell differentiation induced by VND7 ( seiv ) mutants. We found the seiv1 mutant to be a recessive mutant in which ectopic xylem cell differentiation was inhibited, especially in aboveground organs. In seiv1 mutants, a single nucleic acid substitution (G to A) leading to an amino acid substitution (E36K) was present in the gene encoding S -NITROSOGLUTATHIONE REDUCTASE 1 (GSNOR1), which regulates the turnover of the natural NO donor, S -nitrosoglutathione. An in vitro S -nitrosylation assay revealed that VND7 can be S -nitrosylated at Cys264 and Cys320 located near the transactivation activity-related domains, which were shown to be important for transactivation activity of VND7 by transient reporter assay. Our results suggest crucial roles for GSNOR1-regulated protein S -nitrosylation in xylem vessel cell differentiation, partly through the post-translational modification of VND7.