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E2/E3‐independent ubiquitin‐like protein conjugation by Urm1 is directly coupled to cysteine persulfidation

EMBO J. 2022-09; 
Keerthiraju E Ravichandran , Lars Kaduhr , Bozena Skupien-Rabian , Ekaterina Shvetsova , Mikołaj Sokołowski , Ros Cisław Krutyhołowa ,Dominika Kwasna , Cindy Brachmann , Sean Lin , Sebastian Guzman Perez , Piotr Wilk , Manuel Kösters , Przemysław Grudnik , Urszula Jankowska , Sebastian A Leidel , Raffael Schaffrath , Sebastian Glatt
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Post-translational modifications by ubiquitin-like proteins (UBLs) are essential for nearly all cellular processes. Ubiquitin-related modifier 1 (Urm1) is a unique UBL, which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (SCP) and is linked to the noncanonical E1 enzyme Uba4 (ubiquitin-like protein activator 4). While Urm1 has also been observed to conjugate to target proteins like other UBLs, the molecular mechanism of its attachment remains unknown. Here, we reconstitute the covalent attachment of thiocarboxylated Urm1 to various cellular target proteins in vitro, revealing that, unlike other known UBLs, this process is E2/E3-independent and requires oxidative stress. Furthermore, ... More


Urm1; oxidative stress; persulfidation; sulfur transfer; ubiquitin-like.