ArticleRNA (New York, N.Y.)2010
Specificity and kinetics of 23S rRNA modification enzymes RlmH and RluD.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Direct RNA Sequencing Reveals Stress-Dependent and Pathway-Specific rRNA Modification Reprogramming during 50S Biogenesis.Biochemistry · 2026Article
- The gram-positive HtrA, the protease that is also a chaperone.Journal of bacteriology · 2026Review
- Direct RNA Sequencing Reveals Stress-Dependent and Pathway-Specific rRNA Modification Reprogramming During 50S Biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Post-Transcriptional Modifications of the Large Ribosome Subunit Assembly Intermediates inBiochemistry · 2025Article
- Complete list of canonical post-transcriptional modifications in the Bacillus subtilis ribosome and their link to RbgA driven large subunit assembly.Nucleic acids research · 2024Article
- Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024Article
- Loss of Conserved rRNA Modifications in the Peptidyl Transferase Center Leads to Diminished Protein Synthesis and Cell Growth in Budding Yeast.International journal of molecular sciences · 2024Article
- 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
- Methylation of rRNA as a host defense against rampant group II intron retrotransposition.Mobile DNA · 2021Article
- Reductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes.Biomolecules · 2020Article
- Substrate Recognition and Modification by a Pathogen-Associated Aminoglycoside Resistance 16S rRNA Methyltransferase.Antimicrobial agents and chemotherapy · 2017Article
- Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.Scientific reports · 2017Article
- RlmCD-mediated U747 methylation promotes efficient G748 methylation by methyltransferase RlmAII in 23S rRNA in Streptococcus pneumoniae; interplay between two rRNA methylations responsible for telithromycin susceptibility.Nucleic acids research · 2015Article
- tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily.Nucleic acids research · 2015Article
- Quantitative analysis of rRNA modifications using stable isotope labeling and mass spectrometry.Journal of the American Chemical Society · 2014Article
- Pseudouridine: still mysterious, but never a fake (uridine)!RNA biology · 2014Review
- The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL.Nucleic acids research · 2013Article
- Roles of two large serine recombinases in mobilizing the methicillin-resistance cassette SCCmec.Molecular microbiology · 2013Article
- A single methyltransferase YefA (RlmCD) catalyses both m5U747 and m5U1939 modifications in Bacillus subtilis 23S rRNA.Nucleic acids research · 2011Article
Corrections and comments
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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
Along the ribosome assembly pathway, various ribosomal RNA processing and modification reactions take place. Stem-loop 69 in the large subunit of Escherichia coli ribosomes plays a substantial role in ribosome functioning. It contains three highly conserved pseudouridines synthesized by pseudouridine synthase RluD. One of the pseudouridines is further methylated by RlmH. In this paper we show that RlmH has unique substrate specificity among rRNA modification enzymes. It preferentially methylates pseudouridine and less efficiently uridine. Furthermore, RlmH is the only known modification enzyme that is specific to 70S ribosomes. Kinetic parameters determined for RlmH are the following: The apparent K(M) for substrate 70S ribosomes is 0.51 ± 0.06 μM, and for cofactor S-adenosyl-L-methionine 27 ± 3 μM; the k(cat) values are 4.95 ± 1.10 min⁻¹ and 6.4 ± 1.3 min⁻¹, respectively. Knowledge of the substrate specificity and the kinetic parameters of RlmH made it possible to determine the kinetic parameters for RluD as well. The K(M) value for substrate 50S subunits is 0.98 ± 0.18 μM and the k(cat) value is 1.97 ± 0.46 min⁻¹. RluD is the first rRNA pseudouridine synthase to be kinetically characterized. The determined rates of RluD- and RlmH-directed modifications of 23S rRNA are compatible with the rate of 50S assembly in vivo. The fact that RlmH requires 30S subunits demonstrates the dependence of 50S subunit maturation on the simultaneous presence of 30S subunits.
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