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State A of the Trypanosoma brucei mitoribosomal large subunit assembly intermediateState A of the Trypanosoma brucei mitoribosomal large subunit assembly intermediate
Structural highlights
FunctionPublication Abstract from PubMedIn contrast to the bacterial translation machinery, mitoribosomes and mitochondrial translation factors are highly divergent in terms of composition and architecture. There is increasing evidence that the biogenesis of mitoribosomes is an intricate pathway, involving many assembly factors. To better understand this process, we investigated native assembly intermediates of the mitoribosomal large subunit from the human parasite Trypanosoma brucei using cryo-electron microscopy. We identify 28 assembly factors, 6 of which are homologous to bacterial and eukaryotic ribosome assembly factors. They interact with the partially folded rRNA by specifically recognizing functionally important regions such as the peptidyltransferase center. The architectural and compositional comparison of the assembly intermediates indicates a stepwise modular assembly process, during which the rRNA folds toward its mature state. During the process, several conserved GTPases and a helicase form highly intertwined interaction networks that stabilize distinct assembly intermediates. The presented structures provide general insights into mitoribosomal maturation. Structural Insights into the Mechanism of Mitoribosomal Large Subunit Biogenesis.,Jaskolowski M, Ramrath DJF, Bieri P, Niemann M, Mattei S, Calderaro S, Leibundgut M, Horn EK, Boehringer D, Schneider A, Ban N Mol Cell. 2020 Aug 20;79(4):629-644.e4. doi: 10.1016/j.molcel.2020.06.030. Epub, 2020 Jul 16. PMID:32679035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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