Abstract
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.
| Item Type: | Journal article |
|---|---|
| Faculties: | Chemistry and Pharmacy > Department of Biochemistry |
| Subjects: | 500 Science > 540 Chemistry |
| ISSN: | 0014-5793 |
| Language: | English |
| Item ID: | 54151 |
| Date Deposited: | 14. Jun 2018 09:55 |
| Last Modified: | 04. Nov 2020 13:33 |
