Botrytis cinerea-induced F-box protein 1 enhances disease resistance by inhibiting JAO/JOX-mediated jasmonic acid catabolism in Arabidopsis

Abstract

Jasmonic acid (JA) is a crucial phytohormone that regulates plant immunity. The endogenous JA level is determined by the rates of its biosynthesis and catabolism in plants. The activation of JA biosynthesis has been well documented; however, how plants repress JA catabolism upon pathogen infection remains elusive. In this study, we identified and characterized Botrytis cinerea-induced F-box protein 1 (BFP1) in Arabidopsis. The expression of BFP1 was induced by B. cinerea in a JA signaling-dependent manner, and BFP1 protein was critical for plant defense against B. cinerea and plant response to JA. In addition, BFP1 overexpression increased plant defenses against broad-spectrum pathogens without fitness costs. Further experiments demonstrated that BFP1 interacts with and mediates the ubiquitination and degradation of jasmonic acid oxidases (JAOs, also known as jasmonate-induced oxygenases, JOXs), the enzymes that hydroxylate JA to 12OH-JA. Consistent with this, BFP1 affects the accumulation of JA and 12OH-JA during B. cinerea infection. Moreover, mutation of JAO2 complemented the phenotypes of the bfp1 mutant. Collectively, our results unveil a new mechanism used by plants to activate immune responses upon pathogen infection: suppressing JA catabolism.

Keywords: BFP1; JA catabolism; JAO/JOXs; plant immunity; ubiquitination-mediated degradation.