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Journal Article

Cotranslational protein folding on the ribosome monitored in real time.

MPS-Authors
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Holtkamp,  W.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Jäger,  M.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Mittelstät,  J.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Citation

Holtkamp, W., Kokic, G., Jäger, M., Mittelstät, J., Komar, A., & Rodnina, M. V. (2015). Cotranslational protein folding on the ribosome monitored in real time. Science, 250(6264), 1104-1107. doi:10.1126/science.aad0344.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-2266-9
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.