ArticleProceedings of the National Academy of Sciences of the United States of America2010
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 53 citations in OpenAlex.
- THG1L- associated early childhood-onset cerebellar ataxia with atrophy and developmental delay.Neurogenetics · 2026Article
- A comparison ofbioRxiv : the preprint server for biology · 2025Article
- Metal Ion Requirement for Catalysis by 3'-5' RNA Polymerases.Biochemistry · 2025Article
- Thg1 family 3'-5' RNA polymerases as tools for targeted RNA synthesis.RNA (New York, N.Y.) · 2024Article
- Compound heterozygous variants of THG1L result in autosomal recessive cerebellar ataxia.Journal of human genetics · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Modopathies Caused by Mutations in Genes Encoding for Mitochondrial RNA Modifying Enzymes: Molecular Mechanisms and Yeast Disease Models.International journal of molecular sciences · 2023Review
- Human Thg1 displays tRNA-inducible GTPase activity.Nucleic acids research · 2022Article
- Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications.The FEBS journal · 2021Review
- Post-transcriptional regulation in spermatogenesis: all RNA pathways lead to healthy sperm.Cellular and molecular life sciences : CMLS · 2021Review
- Human Mitochondrial RNA Processing and Modifications: Overview.International journal of molecular sciences · 2021Review
- Fidelity of base-pair recognition by a 3'-5' polymerase: mechanism of theRNA (New York, N.Y.) · 2021Article
- Analysis of GTP addition in the reverse (3'-5') direction by human tRNARNA (New York, N.Y.) · 2021Article
- The expanding field of non-canonical RNA capping: new enzymes and mechanisms.Royal Society open science · 2021Review
- Chemical footprinting and kinetic assays reveal dual functions for highly conserved eukaryotic tRNAThe Journal of biological chemistry · 2019Article
- 5'-End sequencing in Saccharomyces cerevisiae offers new insights into 5'-ends of tRNAFEBS letters · 2019Article
- Review
- Article
- Minimal requirements for reverse polymerization and tRNA repair by tRNARNA biology · 2018Article
- Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.Scientific reports · 2017Article
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7 authors at 2 institutions in 1 country.
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Abstract
All known DNA and RNA polymerases catalyze the formation of phosphodiester bonds in a 5' to 3' direction, suggesting this property is a fundamental feature of maintaining and dispersing genetic information. The tRNA(His) guanylyltransferase (Thg1) is a member of a unique enzyme family whose members catalyze an unprecedented reaction in biology: 3'-5' addition of nucleotides to nucleic acid substrates. The 2.3-Å crystal structure of human THG1 (hTHG1) reported here shows that, despite the lack of sequence similarity, hTHG1 shares unexpected structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis. The ability of the same structural architecture to catalyze both 5'-3' and 3'-5' reactions raises important questions concerning selection of the 5'-3' mechanism during the evolution of nucleotide polymerases.
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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.