ArticleNucleic acids research2012
tRNAHis-guanylyltransferase establishes tRNAHis identity.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 50 citations in OpenAlex.
- Characterization and genomic analysis of vB_CoeS_P1, a novel marine bacteriophage, and definition of the new family Estoviridae.Archives of virology · 2026Article
- Inhibition of the integrated stress response rescues a histidyl-tRNA synthetase variant associated with Charcot-Marie-Tooth disease.NAR molecular medicine · 2026Article
- Transfer RNA and small molecule therapeutics for aminoacyl-tRNA synthetase diseases.The FEBS journal · 2025Review
- Yeast models for Charcot-Marie-Tooth disease-causing aminoacyl-tRNA synthetase alleles reveal the cellular basis of disease.IUBMB life · 2025Review
- Transfer RNA supplementation rescues HARS deficiency in a humanized yeast model of Charcot-Marie-Tooth disease.Nucleic acids research · 2024Article
- Characterization of a novel heterozygous variant in the histidyl-tRNA synthetase gene associated with Charcot-Marie-Tooth disease type 2W.IUBMB life · 2024Article
- Thg1 family 3'-5' RNA polymerases as tools for targeted RNA synthesis.RNA (New York, N.Y.) · 2024Article
- Article
- Mechanisms and Delivery of tRNA Therapeutics.Chemical reviews · 2024Review
- tRNA Modifications and Dysregulation: Implications for Brain Diseases.Brain sciences · 2024Review
- A robust method for measuring aminoacylation through tRNA-Seq.bioRxiv : the preprint server for biology · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Histidine supplementation can escalate or rescue HARS deficiency in a Charcot-Marie-Tooth disease model.Human molecular genetics · 2023Article
- Towards a Cure for HARS Disease.Genes · 2023Review
- Human Thg1 displays tRNA-inducible GTPase activity.Nucleic acids research · 2022Article
- Article
- Analysis of GTP addition in the reverse (3'-5') direction by human tRNARNA (New York, N.Y.) · 2021Article
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- Naturally occurring dual recognition of tRNARNA biology · 2019Article
- Genetic Interactions and Molecular Evolution of the Duplicated GenesThe Plant cell · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Histidine transfer RNA (tRNA) is unique among tRNA species as it carries an additional nucleotide at its 5' terminus. This unusual G(-1) residue is the major tRNA(His) identity element, and essential for recognition by the cognate histidyl-tRNA synthetase to allow efficient His-tRNA(His) formation. In many organisms G(-1) is added post-transcriptionally as part of the tRNA maturation process. tRNA(His) guanylyltransferase (Thg1) specifically adds the guanylyate residue by recognizing the tRNA(His) anticodon. Thg1 homologs from all three domains of life have been the subject of exciting research that gave rise to a detailed biochemical, structural and phylogenetic enzyme characterization. Thg1 homologs are phylogenetically classified into eukaryal- and archaeal-type enzymes differing characteristically in their cofactor requirements and specificity. Yeast Thg1 displays a unique but limited ability to add 2-3 G or C residues to mutant tRNA substrates, thus catalyzing a 3' → 5' RNA polymerization. Archaeal-type Thg1, which has been horizontally transferred to certain bacteria and few eukarya, displays a more relaxed substrate range and may play additional roles in tRNA editing and repair. The crystal structure of human Thg1 revealed a fascinating structural similarity to 5' → 3' polymerases, indicating that Thg1 derives from classical polymerases and evolved to assume its specific function in tRNA(His) processing.
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Registered trials
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.