Proteasomal Degradation of JAZ9 by Salt- and Drought-Induced Ring Finger 1 During Pathogen Infection

Abstract

E3 ubiquitin ligase salt- and drought-induced ring finger 1 (SDIR1) plays a novel role in modulating plant immunity against pathogens. The molecular interactors of SDIR1 during pathogen infection are not known. SDIR1-interacting jasmonate zinc-finger inflorescence meristem domain (JAZ) proteins were identified through a yeast two-hybrid (Y2H) screen. Full-length JAZ9 interacts with SDIR1 only in the presence of coronatine (a bacteria-secreted toxin) or jasmonic acid (JA) in a Y2H assay. The bimolecular fluorescence complementation and pull-down assays confirm the in planta interaction of these proteins. JAZ9 proteins, negative regulators of JA-mediated plant defense, were degraded during the pathogen infection by SDIR1 through a proteasomal pathway causing disease susceptibility against hemibiotrophic pathogens.[Graphic: see text] The author(s) have dedicated the work to the public domain under the Creative Commons CC0 “No Rights Reserved” license by waiving all of his or her rights to the work worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law, 2021.

Keywords

• avirulence factors
• bacterial pathogenesis
• ethylene
• genomics
• jasmonic acid
• metabolomics