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-Structure paper
タイトル | Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 3607, Year 2021 |
掲載日 | 2021年6月14日 |
著者 | Ravi Kiran Koripella / Ayush Deep / Ekansh K Agrawal / Pooja Keshavan / Nilesh K Banavali / Rajendra K Agrawal / |
PubMed 要旨 | Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we ...Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF) and a recycling-specific homolog of elongation factor G (EF-G2). These structures clarify an unusual role of a mitochondria-specific segment of RRF, identify the structural distinctions that confer functional specificity to EF-G2, and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2 is markedly different from that of mitochondrial elongation factor EF-G1, suggesting that the two human EF-Gs have evolved diversely to negate the effect of a bacterial antibiotic. |
リンク | Nat Commun / PubMed:34127662 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.15 - 3.49 Å |
構造データ | EMDB-23096, PDB-7l08: EMDB-23114: EMDB-23121, PDB-7l20: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-GDP: ChemComp-GCP: |
由来 |
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キーワード | RIBOSOME (リボソーム) / mtEFG2 and mtRRF / Cryo-EM (低温電子顕微鏡法) / Mammalian (哺乳類) / mito-ribosome / mtEFg2 / mtRRF |