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-Structure paper
タイトル | Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年6月18日 |
著者 | Victor Tobiasson / Alexey Amunts / |
PubMed 要旨 | To understand the steps involved in the evolution of translation, we used , a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ...To understand the steps involved in the evolution of translation, we used , a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins. |
リンク | Elife / PubMed:32553108 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 3.7 Å |
構造データ | EMDB-11032: The mitochondrial ribosome from Tetrahymena thermophila EMDB-11033: EMDB-11034: EMDB-11035: EMDB-11036: EMDB-11037: EMDB-11038: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-FES: ChemComp-ATP: |
由来 |
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キーワード | RIBOSOME / Mitochondrial ribosome / mitochondria / ciliate / tetrahymena |