ArticleThe EMBO journal2022
E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.
Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- URMylation Signaling Pathway in Cancer: Molecular Mechanisms and Therapeutic Opportunities.Current issues in molecular biology · 2026Review
- Post-Chornobyl thyroid papillary carcinomas display distinct pastScientific reports · 2026Article
- NAE1/UBA3-UBE2M are E1 and E2 enzymes for the URM1 modification.Nature communications · 2026Article
- Structural insights into the Urm1-Uba4 pathway and its biological roles.Essays in biochemistry · 2025Review
- Evolutionary conservation of ubiquitin-like protein urmylation as revealed by URM1 gene shuffle from archaea to yeast.Communications biology · 2025Article
- Molecular choreography of E1 enzymes in ubiquitin-like protein cascades: New insights into dynamics and specificity.The Journal of biological chemistry · 2025Review
- Ubiquitin-like Proteins in Autoimmune Diseases: Current Evidence and Therapeutic Opportunities.Immune network · 2025Review
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Tracking of Ubiquitin Signaling through 3.5 Billion Years of Combinatorial Conjugation.International journal of molecular sciences · 2024Review
- Discovery and characterization of noncanonical E2-conjugating enzymes.Science advances · 2024Article
- In the moonlight: non-catalytic functions of ubiquitin and ubiquitin-like proteases.Frontiers in molecular biosciences · 2024Review
- Encystation and Stress Responses under the Control of Ubiquitin-like Proteins in Pathogenic Amoebae.Microorganisms · 2023Review
- The Ubiquitin-like Proteins ofBiomolecules · 2023Review
- E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.The EMBO journal · 2022Article
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17 authors.
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Abstract
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, we present the crystal structures of the peroxiredoxin Ahp1 before and after the covalent attachment of Urm1. Surprisingly, we show that urmylation is accompanied by the transfer of sulfur to cysteine residues in the target proteins, also known as cysteine persulfidation. Our results illustrate the role of the Uba4-Urm1 system as a key evolutionary link between prokaryotic SCPs and the UBL modifications observed in modern eukaryotes.
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