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Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome.
- Source :
-
Science (New York, N.Y.) [Science] 2015 Apr 17; Vol. 348 (6232), pp. 303-8. Date of Electronic Publication: 2015 Apr 02. - Publication Year :
- 2015
-
Abstract
- Mammalian mitochondrial ribosomes (mitoribosomes) synthesize mitochondrially encoded membrane proteins that are critical for mitochondrial function. Here we present the complete atomic structure of the porcine 55S mitoribosome at 3.8 angstrom resolution by cryo-electron microscopy and chemical cross-linking/mass spectrometry. The structure of the 28S subunit in the complex was resolved at 3.6 angstrom resolution by focused alignment, which allowed building of a detailed atomic structure including all of its 15 mitoribosomal-specific proteins. The structure reveals the intersubunit contacts in the 55S mitoribosome, the molecular architecture of the mitoribosomal messenger RNA (mRNA) binding channel and its interaction with transfer RNAs, and provides insight into the highly specialized mechanism of mRNA recruitment to the 28S subunit. Furthermore, the structure contributes to a mechanistic understanding of aminoglycoside ototoxicity.<br /> (Copyright © 2015, American Association for the Advancement of Science.)
- Subjects :
- Aminoglycosides chemistry
Animals
Anti-Bacterial Agents chemistry
Binding Sites
GTP-Binding Proteins chemistry
Humans
Mitochondrial Membranes ultrastructure
Mitochondrial Proteins genetics
Mutation
Nucleic Acid Conformation
Protein Structure, Secondary
RNA, Messenger chemistry
RNA, Ribosomal, 16S chemistry
RNA, Transfer chemistry
Ribosomal Proteins chemistry
Ribosome Subunits, Large chemistry
Ribosome Subunits, Large physiology
Swine
Mitochondria ultrastructure
Mitochondrial Proteins biosynthesis
Ribosome Subunits, Large ultrastructure
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 348
- Issue :
- 6232
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 25837512
- Full Text :
- https://doi.org/10.1126/science.aaa3872