ArticleNucleic acids research2006
THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously folding domain.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- 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
- RNA-binding protein THUMPD2 inhibits proliferation and promotes metastasis in epithelial ovarian cancer.Heliyon · 2024Article
- Review
- A subclass of archaeal U8-tRNA sulfurases requires a [4Fe-4S] cluster for catalysis.Nucleic acids research · 2022Article
- Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022Article
- Review
- Structural and functional insights into Archaeoglobus fulgidus m2G10 tRNA methyltransferase Trm11 and its Trm112 activator.Nucleic acids research · 2020Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112.Nucleic acids research · 2017Article
- Structural and functional analyses of the archaeal tRNA m2G/m22G10 methyltransferase aTrm11 provide mechanistic insights into site specificity of a tRNA methyltransferase that contains common RNA-binding modules.Nucleic acids research · 2016Article
- Crystal structures of the tRNA:m2G6 methyltransferase Trm14/TrmN from two domains of life.Nucleic acids research · 2012Article
- The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N²-methylguanosine at position 6 in tRNA.RNA (New York, N.Y.) · 2012Article
- Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14.Nucleic acids research · 2011Article
- FILTREST3D: discrimination of structural models using restraints from experimental data.Bioinformatics (Oxford, England) · 2010Article
- Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand.RNA (New York, N.Y.) · 2009Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tRNA:m2(2)G10 methyltransferase of Pyrococus abyssi (PAB1283, a member of COG1041) catalyzes the N2,N2-dimethylation of guanosine at position 10 in tRNA. Boundaries of its THUMP (THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases)--containing N-terminal domain [1-152] and C-terminal catalytic domain [157-329] were assessed by trypsin limited proteolysis. An inter-domain flexible region of at least six residues was revealed. The N-terminal domain was then produced as a standalone protein (THUMPalpha) and further characterized. This autonomously folded unit exhibits very low affinity for tRNA. Using protein fold-recognition (FR) methods, we identified the similarity between THUMPalpha and a putative RNA-recognition module observed in the crystal structure of another THUMP-containing protein (ThiI thiolase of Bacillus anthracis). A comparative model of THUMPalpha structure was generated, which fulfills experimentally defined restraints, i.e. chemical modification of surface exposed residues assessed by mass spectrometry, and identification of an intramolecular disulfide bridge. A model of the whole PAB1283 enzyme docked onto its tRNA(Asp) substrate suggests that the THUMP module specifically takes support on the co-axially stacked helices of T-arm and acceptor stem of tRNA and, together with the catalytic domain, screw-clamp structured tRNA. We propose that this mode of interactions may be common to other THUMP-containing enzymes that specifically modify nucleotides in the 3D-core of tRNA.
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