IPR027492
Dual-specificity RNA methyltransferase RlmN
InterPro entry
Short name | RNA_MTrfase_RlmN |
Overlapping homologous superfamilies | |
family relationships |
Description
Dual-specificity RNA methyltransferase RlmN specifically methylates position 2 of adenine 2503 in 23S rRNA, which serves to optimize ribosomal fidelity, and 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
[1, 2, 3].
References
1.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
2.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
3.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
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
Representative structure
6fz6: Crystal Structure of a radical SAM methyltransferase from Sphaerobacter thermophilus