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Transnitrosylation Mediated by the Non-canonical Catalase ROG1 Regulates Nitric Oxide Signaling in Plants.

Developmental cell (2020-04-25)
Lichao Chen, Rong Wu, Jian Feng, Tianpeng Feng, Chun Wang, Jiliang Hu, Ni Zhan, Yansha Li, Xiaohui Ma, Bo Ren, Jian Zhang, Chun-Peng Song, Jiayang Li, Jian-Min Zhou, Jianru Zuo
ABSTRACT

The redox-based protein S-nitrosylation is a conserved mechanism modulating nitric oxide (NO) signaling and has been considered mainly as a non-enzymatic reaction. S-nitrosylation is regulated by the intracellular NO level that is tightly controlled by S-nitrosoglutathione reductase (GSNOR). However, the molecular mechanisms regulating S-nitrosylation selectivity remain elusive. Here, we characterize an Arabidopsis "repressor of" gsnor1 (rog1) mutation that specifically suppresses the gsnor1 mutant phenotype. ROG1, identical to the non-canonical catalase, CAT3, is a transnitrosylase that specifically modifies GSNOR1 at Cys-10. The transnitrosylase activity of ROG1 is regulated by a unique and highly conserved Cys-343 residue. A ROG1C343T mutant displays increased catalase but decreased transnitrosylase activities. Consistent with these results, the rog1 mutation compromises responses to NO under both normal and stress conditions. We propose that ROG1 functions as a transnitrosylase to regulate the NO-based redox signaling in plants.

MATERIALS
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Brand
Product Description

LCD Digital Stopwatch, timing 1/100 sec, accuracy: 0.003%, battery included, pkg of 1 ea
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