Published on July 1, 2014 in J Biol Chem volume None.
PubMed ID: 25074936
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, while 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[& prime]-O-ribose modification to block site-specific cleavage of RNA by DNAzymes to show that MRM1, MRM2 and RNMTL1 are responsible for modification of the human mitochondrial large ribosomal subunit RNA at residues G1145, U1369, and G1370, respectively.