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Almost all abiotic stresses induce reactive oxygen species (ROS) overaccumulation, causing oxidative damages to plant cells. Catalase (CAT) plays a vital role in plant oxidative stress tolerance by scavenging stress-induced excess H 2 O 2 ; thus, the identification of factors regulating catalase function will shed light on the underlying regulatory mechanisms. Here, we identified leucine aminopeptidase 2 ( LAP2 ) as a novel  CAT2 -interacting protein and showed a mutual promotion effect of the two proteins in plant stress responses.  LAP2  has a physical interaction with  CAT2  in plant cells. The loss-of-function mutant of  LAP2 ,  lap2-3 , is hypersensitive to salt or osmotic stress with increased ROS accumulation and malondialdehyde content and decreased catalase activity. The  lap2-3  mutant has less  CAT2  protein levels as  CAT2  protein stability is impaired in the mutant. Scavenging excess ROS by glutathione or overexpressing  CAT2  in the  lap2-3  mutant recovers its hypersensitive phenotype to salt or osmotic stress. Further study showed that  CAT2  promotes  LAP2  hydrolysis activity with leucine-4-methylcoumaryl-7-amides as a substrate  in vivo  and  in vitro , and thus, similar to the  lap2-3  mutant, the  cat2-1  mutant also has lower γ-aminobutyric acid content than the wild type. Together, our study reveals mutual promotion effects of  CAT2  and  LAP2  in conferring plant salt and osmotic stress tolerance.

Mutual Promotion of LAP2 and CAT2 Synergistically Regulates Plant Salt and Osmotic Stress Tolerance