ArticleNucleic acids research2013
The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 44 citations in OpenAlex.
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- New layers of regulation of the general stress response sigma factor RpoS.Frontiers in microbiology · 2024Review
- Escherichia coli tRNA (Gm18) methyltransferase (TrmH) requires the correct localization of its methylation site (G18) in the D-loop for efficient methylation.Journal of biochemistry · 2023Article
- A Preliminary Survey of Transfer RNA Modifications and Modifying Enzymes of the Tropical PlantGenes · 2023Article
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- TheRNA (New York, N.Y.) · 2022Article
- THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.Nucleic acids research · 2021Article
- The occurrence order and cross-talk of different tRNA modifications.Science China. Life sciences · 2021Review
- Tying up the Loose Ends: A Mathematically Knotted Protein.Frontiers in chemistry · 2021Article
- A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.Biochemistry · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- A rationale for tRNA modification circuits in the anticodon loop.RNA (New York, N.Y.) · 2018Review
- Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes.The Journal of biological chemistry · 2018Article
- Review
- Modifications and functional genomics of human transfer RNA.Cell research · 2018Review
- Identification of tRNA nucleoside modification genes critical for stress response and development in rice and Arabidopsis.BMC plant biology · 2017Article
- To Tie or Not to Tie? That Is the Question.Polymers · 2017Review
- TrmL and TusA Are Necessary for rpoS and MiaA Is Required for hfq Expression in Escherichia coli.Biomolecules · 2017Article
- Transfer RNA methyltransferases with a SpoU-TrmD (SPOUT) fold and their modified nucleosides in tRNA.Biomolecules · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike other transfer RNAs (tRNA)-modifying enzymes from the SPOUT methyltransferase superfamily, the tRNA (Um34/Cm34) methyltransferase TrmL lacks the usual extension domain for tRNA binding and consists only of a SPOUT domain. Both the catalytic and tRNA recognition mechanisms of this enzyme remain elusive. By using tRNAs purified from an Escherichia coli strain with the TrmL gene deleted, we found that TrmL can independently catalyze the methyl transfer from S-adenosyl-L-methionine to and isoacceptors without the involvement of other tRNA-binding proteins. We have solved the crystal structures of TrmL in apo form and in complex with S-adenosyl-homocysteine and identified the cofactor binding site and a possible active site. Methyltransferase activity and tRNA-binding affinity of TrmL mutants were measured to identify residues important for tRNA binding of TrmL. Our results suggest that TrmL functions as a homodimer by using the conserved C-terminal half of the SPOUT domain for catalysis, whereas residues from the less-conserved N-terminal half of the other subunit participate in tRNA recognition.
Indexed as
Identifiers
What OpenQuestion holds
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.