ArticleProceedings of the National Academy of Sciences of the United States of America2006
tRNAHis guanylyltransferase catalyzes a 3'-5' polymerization reaction that is distinct from G-1 addition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 55 citations in OpenAlex.
- 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
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Human Thg1 displays tRNA-inducible GTPase activity.Nucleic acids research · 2022Article
- Analysis of GTP addition in the reverse (3'-5') direction by human tRNARNA (New York, N.Y.) · 2021Article
- Fidelity of base-pair recognition by a 3'-5' polymerase: mechanism of theRNA (New York, N.Y.) · 2021Article
- 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
- 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
- The biogenesis pathway of tRNA-derived piRNAs in Bombyx germ cells.Nucleic acids research · 2017Article
- Article
- The structure and function ofThe Journal of biological chemistry · 2017Article
- 5'-Terminal nucleotide variations in human cytoplasmic tRNAHisGUG and its 5'-halves.RNA (New York, N.Y.) · 2017Article
- Repairing tRNA termini: News from the 3' end.RNA biology · 2016Article
- Identification of distinct biological functions for four 3'-5' RNA polymerases.Nucleic acids research · 2016Article
- In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.FEBS letters · 2015Article
- Natural Variation Identifies ICARUS1, a Universal Gene Required for Cell Proliferation and Growth at High Temperatures in Arabidopsis thaliana.PLoS genetics · 2015Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Yeast tRNA(His) guanylyltransferase, Thg1, is an essential protein that adds a single guanine to the 5' end (G(-1)) of tRNA(His). This G(-1) residue is required for aminoacylation of tRNA(His) by histidyl-tRNA synthetase, both in vitro and in vivo. The guanine nucleotide addition reaction catalyzed by Thg1 extends the polynucleotide chain in the reverse (3'-5') direction of other known polymerases, albeit by one nucleotide. Here, we show that alteration of the 3' end of the Thg1 substrate tRNA(His) unleashes an unexpected reverse polymerase activity of wild-type Thg1, resulting in the 3'-5' addition of multiple nucleotides to the tRNA, with efficiency comparable to the G(-1) addition reaction. The addition of G(-1) forms a mismatched G.A base pair at the 5' end of tRNA(His), and, with monophosphorylated tRNA substrates, it is absolutely specific for tRNA(His). By contrast, reverse polymerization forms multiple G.C or C.G base pairs, and, with preactivated tRNA species, it can initiate at positions other than -1 and is not specific for tRNA(His). Thus, wild-type Thg1 catalyzes a templated polymerization reaction acting in the reverse direction of that of canonical DNA and RNA polymerases. Surprisingly, Thg1 can also readily use dNTPs for nucleotide addition. These results suggest that 3'-5' polymerization represents either an uncharacterized role for Thg1 in RNA or DNA repair or metabolism, or it may be a remnant of an earlier catalytic strategy used in nature.
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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.