ArticleNature chemical biology2013
A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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Who cites it
118 citing papers in PubMed, 173 citations in OpenAlex.
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- Anticodon loop remodeling and D-stem shape drive the specific recognition of ANN-decoding tRNAs for t6A modification.Nucleic acids research · 2026Article
- Long-term stability of RNA nucleoside standards for accurate LC-MS quantification.Nucleic acids research · 2026Article
- Structural and biochemical characterization of yeast Tcd enzymes installing the post-transcriptional modification ct6A in tRNA.Nucleic acids research · 2026Article
- RNA modification-mediated multidimensional crosstalk: a novel perspective on gene expression regulation.Genome biology · 2026Review
- Translational regulation by oxidative desulfuration of tRNA modifications.Nature communications · 2026Article
- Purification of post-transcriptionally modified tRNAs for enhanced cell-free translation systems.Nucleic acids research · 2026Article
- ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025Review
- Toward standardized epitranscriptome analytics: an inter-laboratory comparison of mass spectrometric detection and quantification of modified ribonucleosides in human RNA.Nucleic acids research · 2025Article
- Specificity and mechanism of tRNA cleavage by the AriB Toprim nuclease of the PARIS bacterial immune system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- tRNA modification profiling reveals epitranscriptome regulatory networks in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- A tRNA modification with aminovaleramide facilitates AUA decoding in protein synthesis.Nature chemical biology · 2025Article
- The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.bioRxiv : the preprint server for biology · 2024Article
- A highly conserved tRNA modification contributes toMicrobiology spectrum · 2024Article
- Structural insights into the decoding capability of isoleucine tRNAs with lysidine and agmatidine.Nature structural & molecular biology · 2024Article
- Reversible oxidative dimerization of 4-thiouridines in tRNA isolates.RSC chemical biology · 2024Article
- Anticodon stem-loop tRNA modifications influence codon decoding and frame maintenance during translation.Seminars in cell & developmental biology · 2024Review
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58 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N(6)-threonylcarbamoyladenosine (t(6)A) is a universally conserved, essential modified nucleoside found in transfer RNAs (tRNAs) responsible for ANN codons in all three domains of life. t(6)A has a crucial role in maintaining decoding accuracy during protein synthesis. The presence of t(6)A in cellular tRNAs has been well documented for more than four decades. However, under conditions optimized for nucleoside preparation, we detected little t(6)A in tRNAs from Escherichia coli. Instead, we identified a new modified base named 'cyclic t(6)A' (ct(6)A), which is a cyclized active ester with an oxazolone ring. An E1-like enzyme, CsdL (renamed as TcdA), which catalyzes ATP-dependent dehydration of t(6)A to form ct(6)A, was also identified. Two yeast homologs of tcdA, YHR003C (TCD1) and YKL027W (TCD2), were required for ct(6)A formation and respiratory cell growth. ct(6)A was involved in promoting decoding efficiency. Structural modeling suggests that ct(6)A recognizes the first adenine base of ANN codon at the ribosomal A site.
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