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TitleDistinct mechanisms of the human mitoribosome recycling and antibiotic resistance.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 3607, Year 2021
Publish dateJun 14, 2021
AuthorsRavi Kiran Koripella / Ayush Deep / Ekansh K Agrawal / Pooja Keshavan / Nilesh K Banavali / Rajendra K Agrawal /
PubMed AbstractRibosomes 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.
External linksNat Commun / PubMed:34127662 / PubMed Central
MethodsEM (single particle)
Resolution3.15 - 3.49 Å
Structure data

23096

7l08

EMDB-23096, PDB-7l08:
Cryo-EM structure of the human 55S mitoribosome-RRFmt complex.
Method: EM (single particle) / Resolution: 3.49 Å

EMDB-23114:
Cryo-EM structure of the human 55S mitoribosome in complex with RRFmt and EF-G2mt
Method: EM (single particle) / Resolution: 3.49 Å

23121

7l20

EMDB-23121, PDB-7l20:
Cryo-EM structure of the human 39S mitoribosomal subunit in complex with RRFmt and EF-G2mt.
Method: EM (single particle) / Resolution: 3.15 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-GCP:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-PCP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
KeywordsRIBOSOME / mtEFG2 and mtRRF / Cryo-EM / Mammalian / mito-ribosome / mtEFg2 / mtRRF

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