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  Cotranslational protein folding on the ribosome monitored in real time.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2266-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-12C8-E
Genre: Journal Article

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 Creators:
Holtkamp, W.1, Author              
Kokic, G., Author
Jäger, M.1, Author              
Mittelstät, J.1, Author              
Komar, A., Author
Rodnina, M. V.1, Author              
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1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 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.

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Language(s): eng - English
 Dates: 2015-11-27
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.aad0344
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 250 (6264) Sequence Number: - Start / End Page: 1104 - 1107 Identifier: -