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Structure paper

TitleElongational stalling activates mitoribosome-associated quality control.
Journal, issue, pagesScience, Vol. 370, Issue 6520, Page 1105-1110, Year 2020
Publish dateNov 27, 2020
AuthorsNirupa Desai / Hanting Yang / Viswanathan Chandrasekaran / Razina Kazi / Michal Minczuk / V Ramakrishnan /
PubMed AbstractThe human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a ...The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase.
External linksScience / PubMed:33243891 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.4 Å
Structure data

EMDB-11636:
Cryo-EM structure of the human mitoribosome in the rotated-1 state with A/A and P/E mt-tRNAs
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-11637:
Cryo-EM structure of Oxa1L-bound human mitoribosomal large subunit
Method: EM (single particle) / Resolution: 3.1 Å

11641

7a5f

EMDB-11641, PDB-7a5f:
Structure of the stalled human mitoribosome with P- and E-site mt-tRNAs
Method: EM (single particle) / Resolution: 4.4 Å

11642

7a5g

EMDB-11642, PDB-7a5g:
Structure of the elongating human mitoribosome bound to mtEF-Tu.GMPPCP and A/T mt-tRNA
Method: EM (single particle) / Resolution: 4.33 Å

11643

7a5h

EMDB-11643, PDB-7a5h:
Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1
Method: EM (single particle) / Resolution: 3.3 Å

11644

7a5i

EMDB-11644, PDB-7a5i:
Structure of the human mitoribosome with A- P-and E-site mt-tRNAs
Method: EM (single particle) / Resolution: 3.7 Å

11645

7a5j

EMDB-11645, PDB-7a5j:
Structure of the split human mitoribosomal large subunit with P-and E-site mt-tRNAs
Method: EM (single particle) / Resolution: 3.1 Å

11646

7a5k

EMDB-11646, PDB-7a5k:
Structure of the human mitoribosome in the post translocation state bound to mtEF-G1
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

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

ChemComp-SO4:
SULFATE ION

ChemComp-MLI:
MALONATE ION

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SPD:
SPERMIDINE

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

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE

Source
  • homo sapiens (human)
  • thermus thermophilus (strain hb27 / atcc baa-163 / dsm 7039) (bacteria)
  • human (human)
  • thermus thermophilus hb27 (bacteria)
KeywordsRIBOSOME / mitochondrial ribosome / ribosome stalling / cryo-EM

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