My research focus is the protein modification, so-called Urmylation. The evolutionarily conserved, bifunctional ubiquitin-related modifier 1 (Urm1) acts as a sulfur donor for tRNA-Thiolation and as a protein modifier. During Urmylation, the protein Urm1 is transferred to a target protein (e.g. Ahp1) via a conserved signal cascade, which ultimately leads to a covalent bond between the two proteins. The 2-Cys-peroxiredoxin Ahp1 detoxifies the cell from ROS with redox-active thiols and this is probably closely related to its Urm1 acceptor activity. Furthermore, in our project, we are investigating the function and fate of diverse other urmylated proteins.