期刊
SCIENCE
卷 350, 期 6264, 页码 1104-1107出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aad0344
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资金
- Max Planck Society
- Deutsche Forschungsgemeinschaft [FOR1805]
- Human Frontier Science Program [RGP0024-2010]
- Max Planck Institute of Biophysical Chemistry (Gottingen)
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.
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