Using yeast and human cells, the Dohmen group investigates conserved co- and post-translational mechanism of controlling protein quality and function in eukaryotic cells. A first project area is concerned with deciphering the pathway of chaperone-assisted assembly of the proteasome, a conserved high-molecular weight protease with essential functions both in protein quality control and in in post-translational regulation of protein function. A second project area focuses on how post-translational modifications by ubiquitin and the related protein SUMO control protein function. A particular focus here is on understanding the enzymes (SUMO-specific proteases and SUMO-targeted ubiquitin ligases) that control the sumoylated state of proteins. The third project area investigates how the biosynthesis of essential poly-cations, the polyamines, is controlled by co- and post-translational mechanism, which include the regulation of a ribosomal frameshifting event during decoding of ornithine decarboxylase (ODC) antizyme mRNA as well as ubiquitin-dependent and -independent proteolytic control mechanisms controlling the levels of ODC, a critical enzyme in polyamine biosynthesis.