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TitleCotranslational Protein Folding inside the Ribosome Exit Tunnel.
Journal, issue, pagesCell Rep, Vol. 12, Issue 10, Page 1533-1540, Year 2015
Publish dateSep 8, 2015
AuthorsOla B Nilsson / Rickard Hedman / Jacopo Marino / Stephan Wickles / Lukas Bischoff / Magnus Johansson / Annika Müller-Lucks / Fabio Trovato / Joseph D Puglisi / Edward P O'Brien / Roland Beckmann / Gunnar von Heijne /
PubMed AbstractAt what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel ...At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
External linksCell Rep / PubMed:26321634 / PubMed Central
MethodsEM (single particle)
Resolution4.8 Å
Structure data

3079

5a7u

EMDB-3079, PDB-5a7u:
Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel.
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSLATION / PROTEIN FOLDING / RIBOSOME / ZINC FINGER / SECM / TRANSLATIONAL ARREST PEPTIDE / CRYO-EM / SINGLE- MOLECULE STUDIES

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