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

Autor: 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

Publikováno v: Ravichandran, Keerthiraju E; Kaduhr, Lars; Skupien-Rabian, Bozena; Shvetsova, Ekaterina; Sokołowski, Mikołaj; Krutyhołowa, Ros Cisław; Kwasna, Dominika; Brachmann, Cindy; Lin, Sean; Guzman Perez, Sebastian; Wilk, Piotr; Kösters, Manuel; Grudnik, Przemysław; Jankowska, Urszula; Leidel, Sebastian A; Schaffrath, Raffael; Glatt, Sebastian (2022). E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation. The EMBO journal, 41(20), e111318. EMBO Press 10.15252/embj.2022111318

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 (

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