ArticleInternational journal of molecular sciences2015
Distribution of ADAT-Dependent Codons in the Human Transcriptome.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Deciphering APOBEC1 in Avians: unravelling loss events and functional insights.Immunogenetics · 2026Article
- tRNA Modifications and Dysregulation: Implications for Brain Diseases.Brain sciences · 2024Review
- Antibody production relies on the tRNA inosine wobble modification to meet biased codon demand.Science (New York, N.Y.) · 2024Article
- Codon decoding by orthogonal tRNAs interrogates theFrontiers in genetics · 2024Article
- ADATscan - A flexible tool for scanning exomes for wobble inosine-dependent codons reveals a neurological bias for genes enriched in such codons in humans and mice.microPublication biology · 2023Article
- Human tRNAs with inosine 34 are essential to efficiently translate eukarya-specific low-complexity proteins.Nucleic acids research · 2021Article
- Inosine in Biology and Disease.Genes · 2021Review
- tRNA ADENOSINE DEAMINASE 3 is required for telomere maintenance in Arabidopsis thaliana.Plant cell reports · 2020Article
- Identification and rescue of a tRNA wobble inosine deficiency causing intellectual disability disorder.RNA (New York, N.Y.) · 2020Article
- Formation of tRNA Wobble Inosine in Humans Is Disrupted by a Millennia-Old Mutation Causing Intellectual Disability.Molecular and cellular biology · 2019Article
- Codon usage optimization in pluripotent embryonic stem cells.Genome biology · 2019Article
- tRNA deamination by ADAT requires substrate-specific recognition mechanisms and can be inhibited by tRFs.RNA (New York, N.Y.) · 2019Article
- Codon adaptation to tRNAs with Inosine modification at position 34 is widespread among Eukaryotes and present in two Bacterial phyla.RNA biology · 2018Article
- Review
- What Froze the Genetic Code?Life (Basel, Switzerland) · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleotide modifications in the anticodons of transfer RNAs (tRNA) play a central role in translation efficiency, fidelity, and regulation of translation, but, for most of these modifications, the details of their function remain unknown. The heterodimeric adenosine deaminases acting on tRNAs (ADAT2-ADAT3, or ADAT) are enzymes present in eukaryotes that convert adenine (A) to inosine (I) in the first anticodon base (position 34) by hydrolytic deamination. To explore the influence of ADAT activity on mammalian translation, we have characterized the human transcriptome and proteome in terms of frequency and distribution of ADAT-related codons. Eight different tRNAs can be modified by ADAT and, once modified, these tRNAs will recognize NNC, NNU and NNA codons, but not NNG codons. We find that transcripts coding for proteins highly enriched in these eight amino acids (ADAT-aa) are specifically enriched in NNC, NNU and NNA codons. We also show that the proteins most enriched in ADAT-aa are composed preferentially of threonine, alanine, proline, and serine (TAPS). We propose that the enrichment in ADAT-codons in these proteins is due to the similarities in the codons that correspond to TAPS.
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