Proteins are essential functional components of cells, and as such their abundance and activity needs to be tightly controlled through their balanced production, modification and destruction. In eukaryotic organisms, the predominant mechanism for regulated protein degradation (proteolysis) is through the ubiquitin proteasome system (UPS). Here, proteins are marked for turnover by so called E3 ubiquitin ligases that catalyse the addition of ubiquitin molecules to the target protein. Compared to other kingdoms, the number of components linked to the UPS has significantly expanded in plant genomes, highlighting the enhanced importance of this cellular system in the plant lineage.
Daniel will present some of his previous and ongoing collaborative work in this area, with a particular focus on how plants use protein degradation via the N-degron pathway as a mechanism for coordinating cellular processes and sensing and responding to environmental signals and stresses. The primary focus will be on the importance of proteolysis via the N-degron pathway for controlling low-oxygen stress responses through functionally distinct transcriptional and epigenetic regulators. In addition to providing a broad overview of previous work, he will also introduce more recent and unpublished findings linking these N-degron targets to the control of plant stress memory and development.