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Structural basis of mitochondrial translation
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Structural basis of mitochondrial translation
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Journal Article
Structural basis of mitochondrial translation
2020
Overview
Translation of mitochondrial messenger RNA (mt-mRNA) is performed by distinct mitoribosomes comprising at least 36 mitochondria-specific proteins. How these mitoribosomal proteins assist in the binding of mt-mRNA and to what extent they are involved in the translocation of transfer RNA (mt-tRNA) is unclear. To visualize the process of translation in human mitochondria, we report ~3.0 Å resolution structure of the human mitoribosome, including the L7/L12 stalk, and eight structures of its functional complexes with mt-mRNA, mt-tRNAs, recycling factor and additional trans factors. The study reveals a transacting protein module LRPPRC-SLIRP that delivers mt-mRNA to the mitoribosomal small subunit through a dedicated platform formed by the mitochondria-specific protein mS39. Mitoribosomal proteins of the large subunit mL40, mL48, and mL64 coordinate translocation of mt-tRNA. The comparison between those structures shows dynamic interactions between the mitoribosome and its ligands, suggesting a sequential mechanism of conformational changes.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ cryo-EM
/ Humans
/ Mitochondria - ultrastructure
/ Mitochondrial Proteins - biosynthesis
/ Mitochondrial Proteins - genetics
/ Mitochondrial Ribosomes - physiology
/ Mitochondrial Ribosomes - ultrastructure
/ mRNA
/ Mutation
/ Neoplasm Proteins - biosynthesis
/ Neoplasm Proteins - genetics
/ Proteins
/ Ribosomal Proteins - biosynthesis
/ Ribosomal Proteins - genetics
/ ribosome
/ RNA
/ RNA, Mitochondrial - metabolism
/ RNA-Binding Proteins - biosynthesis
/ RNA-Binding Proteins - genetics
/ Structural Biology and Molecular Biophysics
/ tRNA
