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TitleMimicry of Canonical Translation Elongation Underlies Alanine Tail Synthesis in RQC.
Journal, issue, pagesMol Cell, Vol. 81, Issue 1, Page 104-114.e6, Year 2021
Publish dateJan 7, 2021
AuthorsSebastian Filbeck / Federico Cerullo / Helge Paternoga / George Tsaprailis / Claudio A P Joazeiro / Stefan Pfeffer /
PubMed AbstractAborted translation produces large ribosomal subunits obstructed with tRNA-linked nascent chains, which are substrates of ribosome-associated quality control (RQC). Bacterial RqcH, a widely conserved ...Aborted translation produces large ribosomal subunits obstructed with tRNA-linked nascent chains, which are substrates of ribosome-associated quality control (RQC). Bacterial RqcH, a widely conserved RQC factor, senses the obstruction and recruits tRNA to modify nascent-chain C termini with a polyalanine degron. However, how RqcH and its eukaryotic homologs (Rqc2 and NEMF), despite their relatively simple architecture, synthesize such C-terminal tails in the absence of a small ribosomal subunit and mRNA has remained unknown. Here, we present cryoelectron microscopy (cryo-EM) structures of Bacillus subtilis RQC complexes representing different Ala tail synthesis steps. The structures explain how tRNA is selected via anticodon reading during recruitment to the A-site and uncover striking hinge-like movements in RqcH leading tRNA into a hybrid A/P-state associated with peptidyl-transfer. Finally, we provide structural, biochemical, and molecular genetic evidence identifying the Hsp15 homolog (encoded by rqcP) as a novel RQC component that completes the cycle by stabilizing the P-site tRNA conformation. Ala tailing thus follows mechanistic principles surprisingly similar to canonical translation elongation.
External linksMol Cell / PubMed:33259811 / PubMed Central
MethodsEM (single particle)
Resolution2.99 - 3.1 Å
Structure data

11862

7aqc

EMDB-11862, PDB-7aqc:
Structure of the bacterial RQC complex (Decoding State)
Method: EM (single particle) / Resolution: 2.99 Å

11864

7aqd

EMDB-11864, PDB-7aqd:
Structure of the bacterial RQC complex (Translocating State)
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
  • bacillus subtilis (strain 168) (bacteria)
KeywordsRIBOSOME / rqch / rqc / rqc2 / hsp15 / fibronectin-binding protein / NEMF / ribosome-associated quality control / ribosome-associated / 50s / Alanine-tailing

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