Cotranslational protein folding on the ribosome monitored in real time
2015 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Holtkamp, Wolf ; Kokic, Goran ; Jäger, Marcus ; Mittelstaet, Joerg ; Komar, Anton A.; Rodnina, Marina V.
- Abstract
- Protein domains can fold into stable tertiary structures while they are synthesized on the ribosome. We used a high-performance, reconstituted in vitro translation system to investigate the folding of a small five-helix protein domain-the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK-in real time. Our observations show that cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains.
- Issue Date
- 2015
- Journal
- Science
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Language
- English