Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA)

J Biol Chem. 2014 Sep 5;289(36):24936-42. doi: 10.1074/jbc.C114.581868. Epub 2014 Jul 29.


Advances in proteomics and large scale studies of potential mitochondrial proteins have led to the identification of many novel mitochondrial proteins in need of further characterization. Among these novel proteins are three mammalian rRNA methyltransferase family members RNMTL1, MRM1, and MRM2. MRM1 and MRM2 have bacterial and yeast homologs, whereas RNMTL1 appears to have evolved later in higher eukaryotes. We recently confirmed the localization of the three proteins to mitochondria, specifically in the vicinity of mtDNA nucleoids. In this study, we took advantage of the ability of 2'-O-ribose modification to block site-specific cleavage of RNA by DNAzymes to show that MRM1, MRM2, and RNMTL1 are responsible for modification of human large subunit rRNA at residues G(1145), U(1369), and G(1370), respectively.

Keywords: Mitochondria; RNA Methyltransferase; RNA Modification; Ribosomal RNA Processing (rRNA Processing); Ribosome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites / genetics
  • Blotting, Northern
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Methylation
  • Methyltransferases / genetics
  • Methyltransferases / metabolism*
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism*
  • Nuclear Proteins
  • RNA Interference
  • RNA, Ribosomal, 16S / genetics
  • RNA, Ribosomal, 16S / metabolism*
  • Ribosome Subunits, Large / genetics
  • Ribosome Subunits, Large / metabolism*


  • Isoenzymes
  • Mitochondrial Proteins
  • Nuclear Proteins
  • RNA, Ribosomal, 16S
  • MRM1 protein, human
  • MRM2 protein, human
  • MRM3 protein, human
  • Methyltransferases