Poster
Margot Raffeiner
Ruhr University Bochum
Bochum, Nordrhein-Westfalen, Germany
Gautier Langin
Faculty of Biology and Biotechnology, Ruhr-University of Bochum
Bochum, Nordrhein-Westfalen, Germany
Huang Tan
Department of Plant Biochemistry, Centre for Plant Molecular Biology (ZMBP), Eberhard Karls University
Tubingen, Baden-Wurttemberg, Germany
Mirita Franz-Wachtel
Proteome Center Tübingen, University of Tübingen
Tübingen, Baden-Wurttemberg, Germany
Boris Macek
Proteome Center Tübingen, University of Tübingen
Tübingen, Baden-Wurttemberg, Germany
Rosa Lozano-Durán
University of Tübingen
Tübingen, GERMANY
Suayib Uestuen
Ruhr-University Bochum
Bochum, Nordrhein-Westfalen, Germany
Proteotoxic stress, caused by the accumulation of misfolded or excess proteins, threatens cell survival. Eukaryotic cells counter this through protein degradation pathways like the ubiquitin-26S proteasome system (UPS), which is crucial for cellular homeostasis and stress responses. In plants, UPS activity increases during bacterial infections, while pathogens suppress it to enhance virulence. Proteasome activation regulates growth and energy balance in plants. While pathogens manipulate the proteasome, plants may have evolved this interaction as a defense strategy, leveraging the growth-defense trade-off to counter infections.
Here, we identify Arabidopsis DNA-DAMAGE INDUCIBLE 1 (DDI1), a ubiquitin-binding aspartyl protease, as a key regulator of proteotoxic stress and immunity. ddi1 mutants are highly sensitive to proteasome inhibition (e.g., induced by bortezomib) and Pseudomonas syringae pv. tomato (Pst) stress, showing reduced proteasome gene expression, increased ubiquitinated protein accumulation, and enhanced Pst susceptibility. We show that DDI1 cleaves NAC53 and NAC78, transcription factors that activate proteasome genes, promoting their nuclear translocation. Evidence suggests DDI1 also regulates abiotic stress, balancing heat stress and bacterial defense. TurboID proximity labeling supports DDI1’s role in protein degradation pathways during biotic and abiotic stress. Overall, DDI1 links protein degradation, stress adaptation, and plant immunity.