METTL15 interacts with the assembly intermediate of murine mitochondrial small ribosomal subunit to form m4C840 12S rRNA residue.

Animals Cells, Cultured Methylation Methyltransferases / metabolism Mice Mitochondria / enzymology RNA, Mitochondrial / chemistry RNA, Ribosomal / chemistry RNA, Ribosomal, 28S / metabolism Ribosome Subunits, Small, Eukaryotic / chemistry

Journal

Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011

Informations de publication

Date de publication:
20 08 2020
Historique:
accepted: 08 06 2020
revised: 12 05 2020
received: 09 07 2019
pubmed: 24 6 2020
medline: 25 9 2020
entrez: 24 6 2020
Statut: ppublish

Résumé

Mammalian mitochondrial ribosomes contain a set of modified nucleotides, which is distinct from that of the cytosolic ribosomes. Nucleotide m4C840 of the murine mitochondrial 12S rRNA is equivalent to the dimethylated m4Cm1402 residue of Escherichia coli 16S rRNA. Here we demonstrate that mouse METTL15 protein is responsible for the formation of m4C 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.

Identifiants

DOI: 10.1093/nar/gkaa522 PMID: 32573735 PMC: PMC7641309
pubmed: 32573735
pii: 5861404
doi: 10.1093/nar/gkaa522
pmc: PMC7641309
doi:

Substances chimiques

RNA, Mitochondrial 0
RNA, Ribosomal 0
RNA, Ribosomal, 28S 0
RNA, ribosomal, 12S 0
Methyltransferases EC 2.1.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

8022-8034

Informations de copyright

© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

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Auteurs

Ivan Laptev (I)

Center of Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Moscow 143028, Russia.
Department of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.

Ekaterina Shvetsova (E)

Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119992, Russia.

Sergey Levitskii (S)

Faculty of Biology, Lomonosov Moscow State University, Moscow 119992, Russia.

Marina Serebryakova (M)

Center of Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Moscow 143028, Russia.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.

Maria Rubtsova (M)

Center of Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Moscow 143028, Russia.
Department of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia.

Victor Zgoda (V)

Institute of Biomedical Chemistry, Moscow 119435, Russia.

Alexey Bogdanov (A)

Department of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.

Piotr Kamenski (P)

Faculty of Biology, Lomonosov Moscow State University, Moscow 119992, Russia.

Petr Sergiev (P)

Center of Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Moscow 143028, Russia.
Department of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Institute of Functional Genomics, Lomonosov Moscow State University, Moscow 119992, Russia.

Olga Dontsova (O)

Center of Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo, Moscow 143028, Russia.
Department of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia.
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › METTL15 interacts with the assembly...
questionsmedicales.fr › Cellules › Cellules cultivées › METTL15 interacts with the assembly...
questionsmedicales.fr › Métabolisme › Alkylation › Méthylation › METTL15 interacts with the assembly...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › METTL15 interacts with the assembly...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › METTL15 interacts with the assembly...
questionsmedicales.fr › Cellules › Structures cellulaires › Fractions subcellulaires › Mitochondries › METTL15 interacts with the assembly...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › ARN mitochondrial › METTL15 interacts with the assembly...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › ARN ribosomique › METTL15 interacts with the assembly...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › ARN ribosomique › ARN ribosomique 28S › METTL15 interacts with the assembly...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Ribosomes › Sous-unités du ribosome › Petite sous-unité du ribosome › Petite sous-unité du ribosome des eucaryotes › METTL15 interacts with the assembly...