ReviewGenes2023
Transfer RNA Modification Enzymes with a Thiouridine Synthetase, Methyltransferase and Pseudouridine Synthase (THUMP) Domain and the Nucleosides They Produce in tRNA.
Review in Genes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Structure of the NAT10 acetyltransferase and mechanism of tRNA acetylation.Nature communications · 2026Article
- OTTR-seq profiling reveals dynamic tRNA modification landscapes across diverse archaeal species.Genome biology · 2026Article
- 2'-O-methylation-dependent installation of NNature communications · 2026Article
- The Landscape of tRNA Modifications in Archaea.bioRxiv : the preprint server for biology · 2025Article
- A transfer RNA methyltransferase with an unusual domain composition catalyzes 2'-O-methylation at position 6 in tRNA.Nucleic acids research · 2025Article
- RudS: bacterial desulfidase responsible for tRNA 4-thiouridine de-modification.Nucleic acids research · 2024Article
- Review
- Deficiency of Acetyltransferase nat10 in Zebrafish Causes Developmental Defects in the Visual Function.Investigative ophthalmology & visual science · 2024Article
- PEGylated Dmoc phosphoramidites for sensitive oligodeoxynucleotide synthesis.Organic & biomolecular chemistry · 2023Article
- tRNAs at the Virus-Host Interface.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The existence of the thiouridine synthetase, methyltransferase and pseudouridine synthase (THUMP) domain was originally predicted by a bioinformatic study. Since the prediction of the THUMP domain more than two decades ago, many tRNA modification enzymes containing the THUMP domain have been identified. According to their enzymatic activity, THUMP-related tRNA modification enzymes can be classified into five types, namely 4-thiouridine synthetase, deaminase, methyltransferase, a partner protein of acetyltransferase and pseudouridine synthase. In this review, I focus on the functions and structures of these tRNA modification enzymes and the modified nucleosides they produce. Biochemical, biophysical and structural studies of tRNA 4-thiouridine synthetase, tRNA methyltransferases and tRNA deaminase have established the concept that the THUMP domain captures the 3'-end of RNA (in the case of tRNA, the CCA-terminus). However, in some cases, this concept is not simply applicable given the modification patterns observed in tRNA. Furthermore, THUMP-related proteins are involved in the maturation of other RNAs as well as tRNA. Moreover, the modified nucleosides, which are produced by the THUMP-related tRNA modification enzymes, are involved in numerous biological phenomena, and the defects of genes for human THUMP-related proteins are implicated in genetic diseases. In this review, these biological phenomena are also introduced.
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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.