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TitleThe shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateNov 26, 2018
AuthorsRenuka Kudva / Pengfei Tian / Fátima Pardo-Avila / Marta Carroni / Robert B Best / Harris D Bernstein / Gunnar von Heijne /
PubMed AbstractThe ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. ...The ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Δloop ribosomes, while two ~ 100 residue proteins normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Δloop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure.
External linksElife / PubMed:30475203 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

4319

6fu8

EMDB-4319, PDB-6fu8:
uL23 beta hairpin loop deletion of E.coli ribosome
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli o157:h7 (bacteria)
KeywordsRIBOSOMAL PROTEIN / uL23 / loop deletion / ribosomal tunnel

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