ArticleRNA (New York, N.Y.)2008
Identification of pseudouridine methyltransferase in Escherichia coli.
Article in RNA (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 62 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- Mapping the rRNA methylome reveals contributions of methyltransferases to ribosome function and antibiotic sensitivity.bioRxiv : the preprint server for biology · 2026Article
- tRNA modifications in cancer: from molecular mechanisms to clinical translation.Biomarker research · 2026Review
- Post-Transcriptional Modifications of the Large Ribosome Subunit Assembly Intermediates inBiochemistry · 2025Article
- Pseudouridine andRSC chemical biology · 2024Review
- RNA Post-transcriptional Modifications of an Early-Stage Large-Subunit Ribosomal Intermediate.Biochemistry · 2023Article
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- RNA Post-Transcriptional Modifications in Two Large Subunit Intermediates Populated inBiochemistry · 2022Article
- Emergence of the primordial pre-60S from the 90S pre-ribosome.Cell reports · 2022Article
- Analogs ofMolecular biology · 2022Article
- Methylation of rRNA as a host defense against rampant group II intron retrotransposition.Mobile DNA · 2021Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- METTL15 interacts with the assembly intermediate of murine mitochondrial small ribosomal subunit to form m4C840 12S rRNA residue.Nucleic acids research · 2020Article
- Reductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes.Biomolecules · 2020Article
- Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme responsible for acp3U formation at position 47 in Escherichia coli tRNAs.Nucleic acids research · 2020Article
- Comprehensive Functional Analysis ofFrontiers in genetics · 2020Article
- Depletion of S-adenosylmethionine impacts on ribosome biogenesis through hypomodification of a single rRNA methylation.Nucleic acids research · 2019Article
- A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.Biochemistry · 2019Article
- Structural and biochemical analysis of the dual-specificity Trm10 enzyme fromRNA (New York, N.Y.) · 2018Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In ribosomal RNA, modified nucleosides are found in functionally important regions, but their function is obscure. Stem-loop 69 of Escherichia coli 23S rRNA contains three modified nucleosides: pseudouridines at positions 1911 and 1917, and N3 methyl-pseudouridine (m(3)Psi) at position 1915. The gene for pseudouridine methyltransferase was previously not known. We identified E. coli protein YbeA as the methyltransferase methylating Psi1915 in 23S rRNA. The E. coli ybeA gene deletion strain lacks the N3 methylation at position 1915 of 23S rRNA as revealed by primer extension and nucleoside analysis by HPLC. Methylation at position 1915 is restored in the ybeA deletion strain when recombinant YbeA protein is expressed from a plasmid. In addition, we show that purified YbeA protein is able to methylate pseudouridine in vitro using 70S ribosomes but not 50S subunits from the ybeA deletion strain as substrate. Pseudouridine is the preferred substrate as revealed by the inability of YbeA to methylate uridine at position 1915. This shows that YbeA is acting at the final stage during ribosome assembly, probably during translation initiation. Hereby, we propose to rename the YbeA protein to RlmH according to uniform nomenclature of RNA methyltransferases. RlmH belongs to the SPOUT superfamily of methyltransferases. RlmH was found to be well conserved in bacteria, and the gene is present in plant and in several archaeal genomes. RlmH is the first pseudouridine specific methyltransferase identified so far and is likely to be the only one existing in bacteria, as m(3)Psi1915 is the only methylated pseudouridine in bacteria described to date.
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