ArticleThe Journal of biological chemistry2012
Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 51 citations in OpenAlex.
- URMylation Signaling Pathway in Cancer: Molecular Mechanisms and Therapeutic Opportunities.Current issues in molecular biology · 2026Review
- NAE1/UBA3-UBE2M are E1 and E2 enzymes for the URM1 modification.Nature communications · 2026Article
- Altered transposon element-derived genes distort oxygen-free radical scavenger systems in FXD.NAR molecular medicine · 2026Article
- NFS1 Plays a Critical Role in Regulating Ferroptosis Homeostasis.Biomolecules · 2025Review
- Blood-based Transcriptomics Reveal Sex- and Amyloid-Modulated Biology of Plasma pTau217 in Preclinical Alzheimer's Disease.bioRxiv : the preprint server for biology · 2025Article
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Article
- Does the Micronutrient Molybdenum Have a Role in Gestational Complications and Placental Health?Nutrients · 2023Review
- Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking.Antioxidants (Basel, Switzerland) · 2023Review
- The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells.Biomolecules · 2023Article
- Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2.Molecules (Basel, Switzerland) · 2022Review
- tRNA modification dynamics from individual organisms to metaepitranscriptomics of microbiomes.Molecular cell · 2022Review
- Urm1: A Non-Canonical UBL.Biomolecules · 2021Review
- Case Report: Compound Heterozygous Variants inFrontiers in genetics · 2021Article
- Biosynthesis of Sulfur-Containing Small Biomolecules in Plants.International journal of molecular sciences · 2020Review
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Molybdenum cofactor transfer from bacteria to nematode mediates sulfite detoxification.Nature chemical biology · 2019Article
- Matching tRNA modifications in humans to their known and predicted enzymes.Nucleic acids research · 2019Article
- Roles of Elongator Dependent tRNA Modification Pathways in Neurodegeneration and Cancer.Genes · 2018Review
- Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied two pathways that involve the transfer of persulfide sulfur in humans, molybdenum cofactor biosynthesis and tRNA thiolation. Investigations using human cells showed that the two-domain protein MOCS3 is shared between both pathways. MOCS3 has an N-terminal adenylation domain and a C-terminal rhodanese-like domain. We showed that MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C terminus of each protein. MOCS2A and URM1 are β-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. The role of the terminal glycine of MOCS2A and URM1 was examined for the interaction and the cellular localization with MOCS3. Deletion of the C-terminal glycine of either MOCS2A or URM1 resulted in a loss of interaction with MOCS3. Enhanced cyan fluorescent protein and enhanced yellow fluorescent protein fusions of the proteins were constructed, and the fluorescence resonance energy transfer efficiency was determined by the decrease in the donor lifetime. The cellular localization results showed that extension of the C terminus with an additional glycine of MOCS2A and URM1 altered the localization of MOCS3 from the cytosol to the nucleus.
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