Journal
FEBS LETTERS
Volume 590, Issue 5, Pages 655-660Publisher
WILEY
DOI: 10.1002/1873-3468.12098
Keywords
cotranslational protein folding; fast-folding domains; GFP; ribosome exit tunnel; SecM; translational arrest
Funding
- Swiss National Science Foundation
- Novartis Foundation for Biomedical Research
- Knut and Alice Wallenberg Foundation
- Swedish Research Council
- European Research Council [ERC-2008-AdG 232648]
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Cotranslational folding of small protein domains within the ribosome exit tunnel may be an important cellular strategy to avoid protein misfolding. However, the pathway of cotranslational folding has so far been described only for a few proteins, and therefore, it is unclear whether folding in the ribosome exit tunnel is a common feature for small protein domains. Here, we have analyzed nine small protein domains and determined at which point during translation their folding generates sufficient force on the nascent chain to release translational arrest by the SecM arrest peptide, both in vitro and in live E. coli cells. We find that all nine protein domains initiate folding while still located well within the ribosome exit tunnel.
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