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Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance

Author

Listed:
  • 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
    University at Albany)

  • Rajendra K. Agrawal

    (Empire State Plaza
    University at Albany)

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.

Suggested Citation

  • Ravi Kiran Koripella & Ayush Deep & Ekansh K. Agrawal & Pooja Keshavan & Nilesh K. Banavali & Rajendra K. Agrawal, 2021. "Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23726-4
    DOI: 10.1038/s41467-021-23726-4
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