Journal
SCIENCE
Volume 346, Issue 6210, Pages 718-722Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1258026
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Funding
- UK Medical Research Council [MC_U105184332, MC_UP_A025_1013]
- Wellcome Trust [WT096570]
- Agouron Institute
- Jeantet Foundation
- Human Frontiers Science Program
- EU FP7 Marie Curie
- MRC [MC_UP_A025_1012, MC_U105184332, MC_UP_A025_1013] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1013, MC_U105184332, MC_UP_A025_1012] Funding Source: researchfish
- Wellcome Trust [096570/Z/11/Z] Funding Source: researchfish
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Human mitochondrial ribosomes are highly divergent from all other known ribosomes and are specialized to exclusively translate membrane proteins. They are linked with hereditary mitochondrial diseases and are often the unintended targets of various clinically useful antibiotics. Using single-particle cryogenic electron microscopy, we have determined the structure of its large subunit to 3.4 angstrom resolution, revealing 48 proteins, 21 of which are specific to mitochondria. The structure unveils an adaptation of the exit tunnel for hydrophobic nascent peptides, extensive remodeling of the central protuberance, including recruitment of mitochondrial valine transfer RNA (tRNA(Val)) to play an integral structural role, and changes in the tRNA binding sites related to the unusual characteristics of mitochondrial tRNAs.
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