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TitleStructural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.
Journal, issue, pagesMol Cell, Vol. 81, Issue 1, Page 115-126.e7, Year 2021
Publish dateJan 7, 2021
AuthorsCaillan Crowe-McAuliffe / Hiraku Takada / Victoriia Murina / Christine Polte / Sergo Kasvandik / Tanel Tenson / Zoya Ignatova / Gemma C Atkinson / Daniel N Wilson / Vasili Hauryliuk /
PubMed AbstractIn all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, ...In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.
External linksMol Cell / PubMed:33259810
MethodsEM (single particle)
Resolution2.6 - 4.9 Å
Structure data

EMDB-11889, PDB-7as8:
Bacillus subtilis ribosome quality control complex state B. Ribosomal 50S subunit with P-tRNA, RqcH, and RqcP/YabO
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-11890, PDB-7as9:
Bacillus subtilis ribosome-associated quality control complex state A. Ribosomal 50S subunit with peptidyl tRNA in the A/P position and RqcH.
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-11891, PDB-7asa:
Bacillus subtilis ribosome-associated quality control complex state B, multibody refinement focussed on RqcH. Ribosomal 50S subunit with P-tRNA, RqcH, and RqcP/YabO
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-11913:
Bacillus subtilis ribosome-associated quality control complex, state C, derived from RqcH affinity purification.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-11914:
Ribosome-associated quality control complex from Bacillus subtilis, state D. Large ribosomal subunit in complex with P-tRNA and RqcP/YabO.
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-11915:
Bacillus subtilis ribosome-associated quality control complex state B*, derived from RqcH affinity purification.
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-11916:
Bacillus subtilis ribosome-associated quality control complex, state E, derived from RqcP/YabO affinity purification.
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-11917:
Bacillus subtilis ribosome-associated quality control complex with SRP, derived from RqcP/YabO affinity purification.
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-11918:
Bacillus subtilis ribosome-associated quality control complex, state D, derived from RqcP/YabO affinity purification.
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-11919:
Bacillus subtilis ribosome-associated quality control complex, state B, derived from RqcP/YabO affinity purification.
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-11920:
Bacillus subtilis ribosome-associated quality control complex with RsfS, derived from RqcP/YabO affinity purification.
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • bacillus subtilis (strain 168) (bacteria)
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
KeywordsTRANSLATION / 50S / tRNA / RQC / RqcH / peptidyl-tRNA / RqcP / YabO / alanine tailing

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