Consecutive oxidative stress in CATALASE2-deficient Arabidopsis negatively regulates Glycolate Oxidase1 activity through S-nitrosylation.

Abstract

Glycolate oxidase (GOX) is a crucial enzyme of photorespiration involving carbon metabolism and stress responses. It is poorly understood, however, how its activities are modulated in response to oxidative stress elicited by various environmental cues. Analysis of Arabidopsis catalase-defective mutant cat2 revealed that the GOX activities were gradually repressed during the growth, which were accompanied by decreased salicylic acid (SA)-dependent cell death, suggesting photorespiratory H₂O₂ may entrain negative feedback regulation of GOX in an age-dependent manner. Intriguingly, a loss-of-function mutation in GLYCOLATE OXIDASE1 (GOX1) rather than in GOX2 and GOX3 attenuated the SA responses of cat2. We found that GOX1 is S-nitrosylated at Cys-343 during consecutive oxidative stress in the cat2 mutant. Subsequently, increased GOX1-SNO formations may contribute to progressively decreased GOX activities and then compromised photorespiratory H₂O₂ flux, which forms a negative feedback loop limiting the amplified activation of SA-dependent defence responses. Together, the data reveal that GOX S-nitrosylation is involved in the crosstalk between photorespiratory H₂O₂ and NO signalling in the fine-tuning regulation of oxidative stress responses and further highlight that NO-based S-nitrosylation acts as an on-off switch for ROS homeostasis.