Arabidopsis OTU2 deubiquitinates cysteine protease RD21A to enhance clubroot resistance.

ABSTRACT: Clubroot is a major threat to cruciferous crops worldwide, largely due to the complex pathogenesis of its causal agent, Plasmodiophora brassicae, and the limited availability of genetic resistance in plants. Previous research has shown that P. brassicae secretes the E3 ubiquitin ligase PbE3-2, which targets and degrades the Arabidopsis thaliana cysteine protease RD21A to facilitate infection. In this study, we identified a plant defense mechanism that counteracts this pathogen virulence strategy. We found that the A. thaliana deubiquitinating enzyme OTU2, whose expression is upregulated during infection, interacts with RD21A. Notably, OTU2 stabilized RD21A by deubiquitination and inhibited the interaction between PbE3-2 and RD21A. Furthermore, OTU2 overexpression enhanced A. thaliana resis

SUBMITTER: Li C 

PROVIDER: S-EPMC11995443 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature