F
IPR004383

Ribosomal RNA large subunit methyltransferase RlmN/Cfr

InterPro entry
Short namerRNA_lsu_MTrfase_RlmN/Cfr
Overlapping
homologous
superfamilies
 
family relationships

Description

This entry represents the RlmN family, that includes dual-specificity RNA methyltransferase RlmN and ribosomal RNA large subunit methyltransferase Cfr.

Dual-specificity RNA methyltransferase RlmN specifically methylates position 2 of adenine 2503 in 23S rRNA
[3]
. This nucleotide is located in a functionally important region of the ribosome, at the entrance to the nascent peptide exit tunnel, and may thus be involved in the interaction with the nascent peptide. It also methylates position 2 of adenine 37 in tRNAs. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation
[3, 5, 4]
.

Ribosomal RNA large subunit methyltransferase Cfr specifically methylates position 8 of adenine 2503 in 23S rRNA. It can also methylate position 2 of A2503 after the primary methylation is complete, to form 2,8-dimethyladenosine. Cfr confers antibiotic resistance in bacteria. The antibiotic resistance is provided by methylation at the 8 position and is independent of methylation at the 2 position of A2503
[1, 2]
.

References

1.Identification of a plasmid-borne chloramphenicol-florfenicol resistance gene in Staphylococcus sciuri. Schwarz S, Werckenthin C, Kehrenberg C. Antimicrob. Agents Chemother. 44, 2530-3, (2000). View articlePMID: 10952608

2.Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria. Giessing AM, Jensen SS, Rasmussen A, Hansen LH, Gondela A, Long K, Vester B, Kirpekar F. RNA 15, 327-36, (2009). View articlePMID: 19144912

3.The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. Toh SM, Xiong L, Bae T, Mankin AS. RNA 14, 98-106, (2008). View articlePMID: 18025251

4.The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. Benitez-Paez A, Villarroya M, Armengod ME. RNA 18, 1783-95, (2012). View articlePMID: 22891362

5.A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ. Science 332, 604-7, (2011). View articlePMID: 21415317

GO terms

cellular component

  • None

Cross References

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