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The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0426-3716
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).ORCID iD: 0000-0002-7697-6427
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Number of Authors: 72018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e36326Article in journal (Refereed) Published
Abstract [en]

The E. coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Delta loop ribosomes, while two similar to 100 residue proteins normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Delta loop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure.

Place, publisher, year, edition, pages
2018. Vol. 7, article id e36326
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Biological Sciences
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URN: urn:nbn:se:su:diva-163616DOI: 10.7554/eLife.36326ISI: 000453505600001PubMedID: 30475203OAI: oai:DiVA.org:su-163616DiVA, id: diva2:1276722
Available from: 2019-01-08 Created: 2019-01-08 Last updated: 2022-03-23Bibliographically approved

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Kudva, RenukaCarroni, Martavon Heijne, Gunnar

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