InterPro domain: IPR001537

This entry represents a domain found in the spoU protein from E. coli that shows strong similarities to previously characterised 2'-O-methyltransferases [ 1 , 2 ]. The Mrm1 protein of Saccharomyces cerevisiae has been shown to be required for ribose methylation at a universally conserved nucleotide in the peptidyl transferase centre of the mitochondrial large ribosomal RNA (21S rRNA). Cells reduced in this activity were deficient in formation of functional large subunits of the mitochondrial ribosome. The Mrm1 protein catalyzes the site-specific formation of 2'-O-methylguanosine on in vitro transcripts of both mitochondrial 21S rRNA and E. coli 23S rRNA providing evidence for an essential modified nucleotide in rRNA [ 3 ].

1. The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity. Nucleic Acids Res. 25, 4093-7
2. SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases. Nucleic Acids Res. 21, 5519
3. Functional requirement of a site-specific ribose methylation in ribosomal RNA. Science 262, 1886-9