ArticleNature communications2023
Iron-sulfur clusters are involved in post-translational arginylation.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The C-terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity.FEBS open bio · 2026Article
- The response regulator BqsR/CarR controls FeNature communications · 2026Article
- From Iron to Depression: The Crosstalk Between the Periphery and Brain.Neuroscience bulletin · 2026Review
- The iron-sulfur cluster assembly factor FDX2 is required for tumor initiation but not for growth of established tumors in transplantation models.The Journal of biological chemistry · 2026Article
- FeSseqdb: a curated sequence-level database and interpretable machine learning framework for identifying iron-sulfur proteins.BMC bioinformatics · 2026Article
- Iron-sulfur cofactors in nucleic acid metabolism and protein synthesis: Assembly, delivery, and putative roles in cellular and viral systems.The Journal of biological chemistry · 2026Review
- A labile sulfur ligand in a three-cysteine-coordinated [2Fe-2S] cluster mediates sulfide sensing in NreB.Nature communications · 2026Article
- A kinetic mathematical model of comprehensive iron metabolism in a respiring yeast cell: a basic-pathways approach to solving a large system dynamically.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- The response regulator BqsR/CarR controls ferrous iron (FebioRxiv : the preprint server for biology · 2025Article
- ThebioRxiv : the preprint server for biology · 2025Article
- Structure and Mechanism of Aminoacyl-tRNA-Protein L/F- and R-transferases.Journal of molecular biology · 2025Review
- Arginyltransferase1 drives a mitochondria-dependent program to induce cell death.Cell death & disease · 2025Article
- Identification of an Intrinsically Disordered Region (IDR) in Arginyltransferase 1 (ATE1).Biochemistry · 2024Article
- Machine Learning Guided Rational Design of a Non-Heme Iron-Based Lysine Dioxygenase Improves its Total Turnover Number.Chembiochem : a European journal of chemical biology · 2024Article
- Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1).bioRxiv : the preprint server for biology · 2024Article
- Machine learning guided rational design of a non-heme iron-based lysine dioxygenase improves its total turnover number.bioRxiv : the preprint server for biology · 2024Article
- Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.Metallomics : integrated biometal science · 2024Review
- RNA N6-methyladenosine modification-based biomarkers for absorbed ionizing radiation dose estimation.Nature communications · 2023Article
- The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.Nature communications · 2023Article
- The preparation of recombinant arginyltransferase 1 (ATE1) for biophysical characterization.Methods in enzymology · 2023Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Eukaryotic arginylation is an essential post-translational modification that modulates protein stability and regulates protein half-life. Arginylation is catalyzed by a family of enzymes known as the arginyl-tRNA transferases (ATE1s), which are conserved across the eukaryotic domain. Despite their conservation and importance, little is known regarding the structure, mechanism, and regulation of ATE1s. In this work, we show that ATE1s bind a previously undiscovered [Fe-S] cluster that is conserved across evolution. We characterize the nature of this [Fe-S] cluster and find that the presence of the [Fe-S] cluster in ATE1 is linked to its arginylation activity, both in vitro and in vivo, and the initiation of the yeast stress response. Importantly, the ATE1 [Fe-S] cluster is oxygen-sensitive, which could be a molecular mechanism of the N-degron pathway to sense oxidative stress. Taken together, our data provide the framework of a cluster-based paradigm of ATE1 regulatory control.
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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 Socratic graph.