ArticleRNA (New York, N.Y.)2006
tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 63 citations in OpenAlex.
- A comparison ofbioRxiv : the preprint server for biology · 2025Article
- Thg1 family 3'-5' RNA polymerases as tools for targeted RNA synthesis.RNA (New York, N.Y.) · 2024Article
- tRFUniverse: A comprehensive resource for the interactive analyses of tRNA-derived ncRNAs in human cancer.iScience · 2024Article
- The Typical tRNA Co-Expresses Multiple 5' tRNA Halves Whose Sequences and Abundances Depend on Isodecoder and Isoacceptor and Change with Tissue Type, Cell Type, and Disease.Non-coding RNA · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Fidelity of base-pair recognition by a 3'-5' polymerase: mechanism of theRNA (New York, N.Y.) · 2021Article
- The expanding field of non-canonical RNA capping: new enzymes and mechanisms.Royal Society open science · 2021Review
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- On the expanding roles of tRNA fragments in modulating cell behavior.Nucleic acids research · 2020Review
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Genomic innovation of ATD alleviates mistranslation associated with multicellularity in Animalia.eLife · 2020Article
- Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase: Specificity determinants and tRNA-i6A37 profiles.PLoS genetics · 2020Article
- To be or not to be modified: Miscellaneous aspects influencing nucleotide modifications in tRNAs.IUBMB life · 2019Review
- Chemical footprinting and kinetic assays reveal dual functions for highly conserved eukaryotic tRNAThe Journal of biological chemistry · 2019Article
- Review
- A Temporal Order in 5'- and 3'- Processing of Eukaryotic tRNAInternational journal of molecular sciences · 2019Article
- Molecular mechanism of substrate recognition and specificity of tRNARNA (New York, N.Y.) · 2018Article
- TheRNA (New York, N.Y.) · 2018Article
- Minimal requirements for reverse polymerization and tRNA repair by tRNARNA biology · 2018Article
- Human BCDIN3D Is a Cytoplasmic tRNAFrontiers in genetics · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
All eukaryotic tRNA(His) molecules are unique among tRNA species because they require addition of a guanine nucleotide at the -1 position by tRNA(His) guanylyltransferase, encoded in yeast by THG1. This G(-1) residue is both necessary and sufficient for aminoacylation of tRNA by histidyl-tRNA synthetase in vitro and is required for aminoacylation in vivo. Although Thg1 is presumed to be highly specific for tRNA(His) to prevent misacylation of tRNAs, the source of this specificity is unknown. We show here that Thg1 is >10,000-fold more selective for its cognate substrate tRNA(His) than for the noncognate substrate tRNA(Phe). We also demonstrate that the GUG anticodon of tRNA(His) is a crucial Thg1 identity element, since alteration of this anticodon in tRNA(His) completely abrogates Thg1 activity, and the simple introduction of this GUG anticodon to any of three noncognate tRNAs results in significant Thg1 activity. For tRNA(Phe), k(cat)/K(M) is improved by at least 200-fold. Thg1 is the only protein other than aminoacyl-tRNA synthetases that is known to use the anticodon as an identity element to discriminate among tRNA species while acting at a remote site on the tRNA, an unexpected link given the lack of any identifiable sequence similarity between these two families of proteins. Moreover, Thg1 and tRNA synthetases share two other features: They act in close proximity to one another at the top of the tRNA aminoacyl-acceptor stem, and the chemistry of their respective reactions is strikingly similar.
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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.