ArticleRNA (New York, N.Y.)2007
Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Ptch/SPOUT1 methyltransferase deposits an mScience advances · 2024Article
- Molecular Dynamics and Docking Simulations of Homologous RsmE Methyltransferases Hints at a General Mechanism for Substrate Release upon Uridine Methylation on 16S rRNA.International journal of molecular sciences · 2023Article
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- Depletion of S-adenosylmethionine impacts on ribosome biogenesis through hypomodification of a single rRNA methylation.Nucleic acids research · 2019Article
- Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases.Protein science : a publication of the Protein Society · 2017Article
- Substrate Recognition and Modification by a Pathogen-Associated Aminoglycoside Resistance 16S rRNA Methyltransferase.Antimicrobial agents and chemotherapy · 2017Article
- Catalytic promiscuity of a bacterial α-N-methyltransferase.FEBS letters · 2012Article
- S-adenosylmethionine-binding properties of a bacterial phospholipid N-methyltransferase.Journal of bacteriology · 2011Article
- Structural and functional characterization of Rv2966c protein reveals an RsmD-like methyltransferase from Mycobacterium tuberculosis and the role of its N-terminal domain in target recognition.The Journal of biological chemistry · 2011Article
- The aminoglycoside resistance methyltransferases from the ArmA/Rmt family operate late in the 30S ribosomal biogenesis pathway.RNA (New York, N.Y.) · 2011Article
- Specificity and kinetics of 23S rRNA modification enzymes RlmH and RluD.RNA (New York, N.Y.) · 2010Article
- Subribosomal particle analysis reveals the stages of bacterial ribosome assembly at which rRNA nucleotides are modified.RNA (New York, N.Y.) · 2010Article
- Deconstructing ribosome construction.Trends in biochemical sciences · 2009Review
- Identification of pseudouridine methyltransferase in Escherichia coli.RNA (New York, N.Y.) · 2008Article
- Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm.Journal of bacteriology · 2008Article
- RluD, a highly conserved pseudouridine synthase, modifies 50S subunits more specifically and efficiently than free 23S rRNA.RNA (New York, N.Y.) · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The small ribosome subunit of Escherichia coli contains 10 base-methylated sites distributed in important functional regions. At present, seven enzymes responsible for methylation of eight bases are known, but most of them have not been well characterized. One of these enzymes, RsmE, was recently identified and shown to specifically methylate U1498. Here we describe the enzymatic properties and substrate specificity of RsmE. The enzyme forms dimers in solution and is most active in the presence of 10-15 mM Mg(2+) and 100 mM NH(4)Cl at pH 7-9; however, in the presence of spermidine, Mg(2+) is not required for activity. While small ribosome subunits obtained from an RsmE deletion strain can be methylated by purified RsmE, neither 70S ribosomes nor 50S subunits are active. Likewise, 16S rRNA obtained from the mutant strain, synthetic 16S rRNA, and 3' minor domain RNA are all very poor or inactive as substrates. 30S particles partially depleted of proteins by treatment with high concentrations of LiCl or in vitro reconstituted intermediate particles also show little or no methyl acceptor activity. Based on these data, we conclude that RsmE requires a highly structured ribonucleoprotein particle as a substrate for methylation, and that methylation events in the 3' minor domain of 16S rRNA probably occur late during 30S ribosome assembly.
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