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Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress

The posttranslational modification of proteins with ubiquitin and ubiquitin-like proteins (collectively referred to as UBLs) has emerged as a major regulatory mechanism in eukaryotes. UBLs are characterized by a core β-grasp fold and an essential carboxy terminal glycine within a di-glycine motif (1). These features are also found in several prokaryotic sulfur carriers, suggestive of an evolutionary relationship to UBLs (2–5). A case in point is the UBL Urm1 (ubiquitin-related modifier 1). Urm1 is known to be conjugated to the peroxiredoxin Ahp1 (6), but its sequence and structure more closely resembles bacterial sulfur carrier proteins (7). In PNAS, work by Van der Veen et al. provides important insight into the mechanism of Urm1 conjugation that highlights its position as an ancient UBL in eukaryotes and solidifies its roles as a posttranslational protein modifier involved in oxidative stress response mechanisms (8).