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

@article{Petroski2011Urm1CS,
  title={Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress.},
  author={Matthew D. Petroski and Guy Salvesen and Dieter A. Wolf},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 5},
  pages={1749-50}
}
T he 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… CONTINUE READING