Mutational analysis of protein folding inside the ribosome exit tunnel
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
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.
arrest peptide, cotranslational protein folding, ribosome
IdentifiersURN: urn:nbn:se:su:diva-141262DOI: 10.1002/1873-3468.12504ISI: 000393957400017PubMedID: 27925654OAI: oai:DiVA.org:su-141262DiVA: diva2:1088161