ArticleNucleic acids research2016
Identification of distinct biological functions for four 3'-5' RNA polymerases.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 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
- 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
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
- 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
- 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
- Repairing tRNA termini: News from the 3' end.RNA biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The superfamily of 3'-5' polymerases synthesize RNA in the opposite direction to all other DNA/RNA polymerases, and its members include eukaryotic tRNA(His) guanylyltransferase (Thg1), as well as Thg1-like proteins (TLPs) of unknown function that are broadly distributed, with family members in all three domains of life. Dictyostelium discoideum encodes one Thg1 and three TLPs (DdiTLP2, DdiTLP3 and DdiTLP4). Here, we demonstrate that depletion of each of the genes results in a significant growth defect, and that each protein catalyzes a unique biological reaction, taking advantage of specialized biochemical properties. DdiTLP2 catalyzes a mitochondria-specific tRNA(His) maturation reaction, which is distinct from the tRNA(His) maturation reaction typically catalyzed by Thg1 enzymes on cytosolic tRNA. DdiTLP3 catalyzes tRNA repair during mitochondrial tRNA 5'-editing in vivo and in vitro, establishing template-dependent 3'-5' polymerase activity of TLPs as a bona fide biological activity for the first time since its unexpected discovery more than a decade ago. DdiTLP4 is cytosolic and, surprisingly, catalyzes robust 3'-5' polymerase activity on non-tRNA substrates, strongly implying further roles for TLP 3'-5' polymerases in eukaryotes.
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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.