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Structure of the large ribosomal subunit from human mitochondria.

ABSTRACT: 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.

SUBMITTER: Brown A

PROVIDER: S-EPMC4246062 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Structure of the large ribosomal subunit from human mitochondria.

Brown Alan A Amunts Alexey A Bai Xiao-Chen XC Sugimoto Yoichiro Y Edwards Patricia C PC Murshudov Garib G Scheres Sjors H W SHW Ramakrishnan V V

Science (New York, N.Y.) 20141002 6210

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 unveil ...[more]

PMID: 25278503

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