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dc.contributor.authorGreber, BJ
dc.contributor.authorBieri, P
dc.contributor.authorLeibundgut, M
dc.contributor.authorLeitner, A
dc.contributor.authorAebersold, R
dc.contributor.authorBoehringer, D
dc.contributor.authorBan, N
dc.date.accessioned2020-10-05T08:49:43Z
dc.date.issued2015-04-17
dc.identifier.citationScience (New York, N.Y.), 2015, 348 (6232), pp. 303 - 308
dc.identifier.issn0036-8075
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4123
dc.identifier.eissn1095-9203
dc.identifier.doi10.1126/science.aaa3872
dc.description.abstractMammalian 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.
dc.formatPrint-Electronic
dc.format.extent303 - 308
dc.languageeng
dc.language.isoeng
dc.publisherAMER ASSOC ADVANCEMENT SCIENCE
dc.rights.urihttps://www.rioxx.net/licenses/all-rights-reserved
dc.subjectMitochondria
dc.subjectAnimals
dc.subjectSwine
dc.subjectHumans
dc.subjectGTP-Binding Proteins
dc.subjectAminoglycosides
dc.subjectMitochondrial Proteins
dc.subjectRibosomal Proteins
dc.subjectRNA, Messenger
dc.subjectRNA, Ribosomal, 16S
dc.subjectRNA, Transfer
dc.subjectAnti-Bacterial Agents
dc.subjectBinding Sites
dc.subjectNucleic Acid Conformation
dc.subjectProtein Structure, Secondary
dc.subjectMutation
dc.subjectMitochondrial Membranes
dc.subjectRibosome Subunits, Large
dc.titleRibosome. The complete structure of the 55S mammalian mitochondrial ribosome.
dc.typeJournal Article
dcterms.dateAccepted2015-03-06
rioxxterms.versionofrecord10.1126/science.aaa3872
rioxxterms.licenseref.urihttps://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2015-04-02
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfScience (New York, N.Y.)
pubs.issue6232
pubs.notesNo embargo
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume348
pubs.embargo.termsNo embargo
dc.contributor.icrauthorGreber, Basil


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