ArticleNucleic acids research2019
Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Transcriptome Analysis Reveals the Potential Mechanism of MAP34-B TargetingMicroorganisms · 2026Article
- Evolutionary conservation of ubiquitin-like protein urmylation as revealed by URM1 gene shuffle from archaea to yeast.Communications biology · 2025Article
- Autophosphorylation of conserved yeast and human casein kinase 1 isozymes regulates Elongator-dependent tRNA modifications.Nucleic acids research · 2025Article
- tRNA binding to Kti12 is crucial for wobble uridine modification by Elongator.Nucleic acids research · 2025Article
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Cryo-EM structures of the human Elongator complex at work.Nature communications · 2024Article
- Evolutionary Conservation in Protein-Protein Interactions and Structures of the Elongator Sub-Complex ELP456 fromInternational journal of molecular sciences · 2024Article
- Yeast geneMicrobial cell (Graz, Austria) · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Cryo-EM structure of the fully assembled Elongator complex.Nucleic acids research · 2023Article
- Transcriptomic response of bioengineered human cartilage to parabolic flight microgravity is sex-dependent.NPJ microgravity · 2023Article
- E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.The EMBO journal · 2022Article
- AtELP4 a subunit of the Elongator complex inFrontiers in plant science · 2022Article
- How Elongator Acetylates tRNA Bases.International journal of molecular sciences · 2020Review
- Plant Elongator-Protein Complex of Diverse Activities Regulates Growth, Development, and Immune Responses.International journal of molecular sciences · 2020Review
- Fungal Kti12 proteins display unusual linker regions and unique ATPase p-loops.Current genetics · 2020Article
- Misactivation of multiple starvation responses in yeast by loss of tRNA modifications.Nucleic acids research · 2020Article
- Effects of Peptide Thanatin on the Growth and Transcriptome ofFrontiers in microbiology · 2020Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12's nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar mechanisms of tRNA binding and show tRNASec-dependent ATPase activity. In addition, we demonstrate that Kti12 binds directly to Elongator and that ATP hydrolysis is crucial for Elongator to maintain proper tRNA anticodon modification levels in vivo. In summary, our data reveal a hitherto uncharacterized link between two translational control pathways that regulate selenocysteine incorporation and affect ribosomal tRNA selection via specific tRNA modifications.
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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.