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

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.
Ken-Wing Lee 1,  Daniel F Bogenhagen 2
Affiliations

Affiliations

  • 1 From the Department of Pharmacological Sciences, Stony Brook University, Stony Brook, New York 11794-8651.
  • 2 From the Department of Pharmacological Sciences, Stony Brook University, Stony Brook, New York 11794-8651 daniel.bogenhagen@stonybrook.edu.
PMID: 25074936 DOI: 10.1074/jbc.C114.581868
Abstract

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.

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