ArticleNucleic acids research2013
Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 75 citations in OpenAlex.
- Anticodon loop remodeling and D-stem shape drive the specific recognition of ANN-decoding tRNAs for t6A modification.Nucleic acids research · 2026Article
- Catalytic and regulatory basis of tRNA tNature communications · 2026Article
- Hidden Diversity in Yeast tRNAs: Comparative Genomics and Modification Mapping in a Eukaryotic Subphylum.bioRxiv : the preprint server for biology · 2026Article
- Structures of KEOPS bound to tRNA reveal functional roles of the kinase Bud32.Nature communications · 2024Article
- The Last Universal Common Ancestor of Ribosome-Encoding Organisms: Portrait of LUCA.Journal of molecular evolution · 2024Review
- Molecular basis of A. thaliana KEOPS complex in biosynthesizing tRNA t6A.Nucleic acids research · 2024Article
- Multifaceted roles of t6A biogenesis in efficiency and fidelity of mitochondrial gene expression.Nucleic acids research · 2024Article
- Article
- Case Report: Novel compound heterozygousFrontiers in pediatrics · 2024Article
- Structure-function analysis of an ancient TsaD-TsaC-SUA5-TcdA modular enzyme reveals a prototype of tRNA t6A and ct6A synthetases.Nucleic acids research · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Epitranscriptomics in metabolic disease.Nature metabolism · 2023Review
- Article
- A paralog of Pcc1 is the fifth core subunit of the KEOPS tRNA-modifying complex in Archaea.Nature communications · 2023Article
- The universal Sua5/TsaC family evolved different mechanisms for the synthesis of a key tRNA modification.Frontiers in microbiology · 2023Article
- Unraveling the Pathobiological Role of the Fungal KEOPS Complex in Cryptococcus neoformans.mBio · 2022Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- tBiomolecules · 2022Article
- Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.Molecular microbiology · 2022Article
- Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.Biomolecules · 2022Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N(6)-threonylcarbamoyladenosine (t(6)A) is a universal tRNA modification essential for normal cell growth and accurate translation. In Archaea and Eukarya, the universal protein Sua5 and the conserved KEOPS/EKC complex together catalyze t(6)A biosynthesis. The KEOPS/EKC complex is composed of Kae1, a universal metalloprotein belonging to the ASHKA superfamily of ATPases; Bud32, an atypical protein kinase and two small proteins, Cgi121 and Pcc1. In this study, we investigated the requirement and functional role of KEOPS/EKC subunits for biosynthesis of t(6)A. We demonstrated that Pcc1, Kae1 and Bud32 form a minimal functional unit, whereas Cgi121 acts as an allosteric regulator. We confirmed that Pcc1 promotes dimerization of the KEOPS/EKC complex and uncovered that together with Kae1, it forms the tRNA binding core of the complex. Kae1 binds l-threonyl-carbamoyl-AMP intermediate in a metal-dependent fashion and transfers the l-threonyl-carbamoyl moiety to substrate tRNA. Surprisingly, we found that Bud32 is regulated by Kae1 and does not function as a protein kinase but as a P-loop ATPase possibly involved in tRNA dissociation. Overall, our data support a mechanistic model in which the final step in the biosynthesis of t(6)A relies on a strictly catalytic component, Kae1, and three partner proteins necessary for dimerization, tRNA binding and regulation.
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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.