ArticleProceedings of the National Academy of Sciences of the United States of America2010
Template-dependent 3'-5' nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life.
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 42 papers.
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42 citing papers in PubMed, 53 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
- A mechanistic model of primer synthesis from catalytic structures of DNA polymerase α-primase.Nature structural & molecular biology · 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
- 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
- Naturally occurring dual recognition of tRNARNA biology · 2019Article
- 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
- Minimal requirements for reverse polymerization and tRNA repair by tRNARNA biology · 2018Article
- Evolutionary gain of highly divergent tRNA specificities by two isoforms of human histidyl-tRNA synthetase.Cellular and molecular life sciences : CMLS · 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
- Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.Science advances · 2016Article
- In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.FEBS letters · 2015Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of an additional 5' guanosine residue (G(-1)) is a unique feature of tRNA(His). G(-1) is incorporated posttranscriptionally in eukarya via an unusual 3'-5' nucleotide addition reaction catalyzed by the tRNA(His) guanylyltransferase (Thg1). Yeast Thg1 catalyzes an unexpected second activity: Watson-Crick-dependent 3'-5' nucleotide addition that occurs in the opposite direction to nucleotide addition by all known DNA and RNA polymerases. This discovery led to the hypothesis that there are alternative roles for Thg1 family members that take advantage of this unusual enzymatic activity. Here we show that archaeal homologs of Thg1 catalyze G(-1) addition, in vitro and in vivo in yeast, but only in a templated reaction, i.e. with tRNA(His) substrates that contain a C(73) discriminator nucleotide. Because tRNA(His) from archaea contains C(73), these findings are consistent with a physiological function for templated nucleotide addition in archaeal tRNA(His) maturation. Moreover, unlike yeast Thg1, archaeal Thg1 enzymes also exhibit a preference for template-dependent U(-1) addition to A(73)-containing tRNA(His). Taken together, these results demonstrate that Watson-Crick template-dependent 3'-5' nucleotide addition is a shared catalytic activity exhibited by Thg1 family members from multiple domains of life, and therefore, that this unusual reaction may constitute an ancestral activity present in the earliest members of the Thg1 enzyme family.
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