Oxidative post-translational modification of catalase confers salt stress acclimatization by regulating H2O2 homeostasis in Malus hupehensis

Reactive oxygen species (ROS) play an essential role as both signaling molecule and damage agent during salt stress. As a signaling molecule, proper accumulation of H2O2 is crucial to trigger stress response and enhance stress tolerance. However, the dynamic regulation mechanism of H2O2 remains unclear. Here, we show that MhCAT2 (catalase 2 in Malus hupehensis) undergoes oxidative modification in an O2•--dependent manner and that oxidation at His225 residue reduces the MhCAT2 activity. Furthermore, the substitution of His225 with Tyr weakens the activity of MhCAT2. The oxidation modification provides a post-translational brake mechanism for the excessive scavenging of H2O2 caused by salt stress-induced catalase (CAT) over-expression. Overall, this finding provides mechanistic insights on stress tolerance augmentation by an O2•--mediated switch that regulates H2O2 homeostasis in Malus hupehensis. •We identified the mechanism of decreased CAT2 activity in Malus hupehensis under salt stress.•MhCAT2 undergoes oxidative modification in a O2·--dependent manner, causing its reduced activity.•The substitution of His225 with Tyr weakens the activity of MhCAT2.•The oxidation modification of catalase provided a post-translational brake mechanism for the excessive scavenging of H2O2.