ArticleNucleic acids research2018
The Uba4 domain interplay is mediated via a thioester that is critical for tRNA thiolation through Urm1 thiocarboxylation.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- Stress Granule-Associated ZmCTU2 Confers Thermotolerance in Maize via Coordinated Regulation of Proteostasis and ROS Homeostasis.Plant biotechnology journal · 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
- Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins.npj metabolic health and disease · 2025Article
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Article
- Phage defence system CBASS is regulated by a prokaryotic E2 enzyme that imitates the ubiquitin pathway.Nature microbiology · 2024Article
- The Ubiquitin-like Proteins ofBiomolecules · 2023Review
- Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking.Antioxidants (Basel, Switzerland) · 2023Review
- E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.The EMBO journal · 2022Article
- Uba1: A Potential Ubiquitin-like Activator Protein of Urm1 inInternational journal of molecular sciences · 2022Article
- Involvement of Urm1, a Ubiquitin-Like Protein, in the Regulation of Oxidative Stress Response of Toxoplasma gondii.Microbiology spectrum · 2022Article
- tRNA modification dynamics from individual organisms to metaepitranscriptomics of microbiomes.Molecular cell · 2022Review
- Urm1, not quite a ubiquitin-like modifier?Microbial cell (Graz, Austria) · 2021Article
- Urm1: A Non-Canonical UBL.Biomolecules · 2021Review
- Natural variations of SLG1 confer high-temperature tolerance in indica rice.Nature communications · 2020Article
- Molecular basis for the bifunctional Uba4-Urm1 sulfur-relay system in tRNA thiolation and ubiquitin-like conjugation.The EMBO journal · 2020Article
- Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast.Redox biology · 2020Article
- Oxygen-dependent bond formation with FIH regulates the activity of the client protein OTUB1.Redox biology · 2019Article
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic ubiquitin-like proteins (UBLs) have evolved from prokaryotic sulfur-carrier proteins (SCPs). Ubiquitin related modifier 1 (Urm1) shares biochemical and structural features of UBLs and SCPs and is essential for 2-thiolation of cytoplasmic tRNA. This chemical modification of wobble uridine is highly conserved amongst species and is achieved via Urm1 thiocarboxylation by the non-canonical ubiquitin activating 4 enzyme (Uba4), which contains an E1- and a Rhodanese (RHD) domain. While the RHD catalyzes the last step in Urm1-thiocarboxylate formation, the previous steps in Urm1 activation and the interplay between the two domains have remained elusive. To define the underlying mechanism, we established an Urm1 in vitro thiocarboxylation assay, which combined with structure-function and chemical profiling analyses revealed a critical thioester linkage between Urm1 and Uba4 residue Cys225. This linkage is indispensable for the Urm1 intramolecular transfer between the two domains of Uba4 and it is thus, essential for tRNA thiolation in vivo. These findings contribute to a deeper understanding of UBL evolution.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.