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Small protein domains fold inside the ribosome exit tunnel
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Number of Authors: 3
2016 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 590, no 5, 655-660 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2016. Vol. 590, no 5, 655-660 p.
Keyword [en]
cotranslational protein folding, fast-folding domains, GFP, ribosome exit tunnel, SecM, translational arrest
National Category
Biological Sciences
URN: urn:nbn:se:su:diva-128511DOI: 10.1002/1873-3468.12098ISI: 000371402700007OAI: diva2:917426
Available from: 2016-04-06 Created: 2016-03-30 Last updated: 2016-04-06Bibliographically approved

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von Heijne, Gunnar
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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