METTL15 interacts with the assembly intermediate of murine mitochondrial small ribosomal subunit to form m4C840 12S rRNA residue. Issue 14 (23rd June 2020)

• Record Type: Journal Article
• Authors: Laptev, Ivan; Shvetsova, Ekaterina; Levitskii, Sergey; Serebryakova, Marina; Rubtsova, Maria; Zgoda, Victor; Bogdanov, Alexey; Kamenski, Piotr; Sergiev, Petr; Dontsova, Olga
• Is Part Of: Nucleic acids research. Volume 48:Issue 14(2020)
• Page Start: 8022
• Page End: 8034
• Publication Date: 2020-06-23
• Subjects: Nucleic acids -- Periodicals; Molecular biology -- Periodicals; 572.805
• DOI: 10.1093/nar/gkaa522
• Languages: English
• ISSNs: 0305-1048

Abstract

Abstract: Mammalian mitochondrial ribosomes contain a set of modified nucleotides, which is distinct from that of the cytosolic ribosomes. Nucleotide m 4 C840 of the murine mitochondrial 12S rRNA is equivalent to the dimethylated m 4 Cm1402 residue of Escherichia coli 16S rRNA. Here we demonstrate that mouse METTL15 protein is responsible for the formation of m 4 C residue of the 12S rRNA. Inactivation of Mettl15 gene in murine cell line perturbs the composition of mitochondrial protein biosynthesis machinery. Identification of METTL15 interaction partners revealed that the likely substrate for this RNA methyltransferase is an assembly intermediate of the mitochondrial small ribosomal subunit containing an assembly factor RBFA.