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Mutational analysis of protein folding inside the ribosome exit tunnel
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Number of Authors: 4
2017 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 591, no 1, 155-163 p.Article in journal (Refereed) Published
Abstract [en]

Recent work has demonstrated that cotranslational folding of proteins or protein domains in, or in the immediate vicinity of, the ribosome exit tunnel generates a pulling force on the nascent polypeptide chain that can be detected using a so-called translational arrest peptide (AP) engineered into the nascent chain as a force sensor. Here, we show that AP-based force measurements combined with systematic Ala and Trp scans of a zinc-finger domain that folds in the exit tunnel can be used to identify the residues that are critical for intraribosomal folding. Our results suggest a general approach to characterize the folded state(s) that may form as a protein domain moves progressively down the ribosome exit tunnel.

Place, publisher, year, edition, pages
2017. Vol. 591, no 1, 155-163 p.
Keyword [en]
arrest peptide, cotranslational protein folding, ribosome
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-141262DOI: 10.1002/1873-3468.12504ISI: 000393957400017PubMedID: 27925654OAI: oai:DiVA.org:su-141262DiVA: diva2:1088161
Available from: 2017-04-11 Created: 2017-04-11 Last updated: 2017-04-11Bibliographically approved

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Farías-Rico, José Arcadiovon Heijne, Gunnar
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