Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance

Ravi Kiran Koripella, Ayush Deep, Ekansh K. Agrawal, Pooja Keshavan, Nilesh K. Banavali and Rajendra K. Agrawal ()
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Ravi Kiran Koripella: Empire State Plaza
Ayush Deep: Empire State Plaza
Ekansh K. Agrawal: Empire State Plaza
Pooja Keshavan: Empire State Plaza
Nilesh K. Banavali: Empire State Plaza
Rajendra K. Agrawal: Empire State Plaza

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract 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 (RRFmt) and a recycling-specific homolog of elongation factor G (EF-G2mt). These structures clarify an unusual role of a mitochondria-specific segment of RRFmt, identify the structural distinctions that confer functional specificity to EF-G2mt, 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-G2mt is markedly different from that of mitochondrial elongation factor EF-G1mt, suggesting that the two human EF-Gmts have evolved diversely to negate the effect of a bacterial antibiotic.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23726-4

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DOI: 10.1038/s41467-021-23726-4

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