Mutational analysis of protein folding inside the ribosome exit tunnel.

Farías-Rico JA, Goetz SK, Marino J, von Heijne G

FEBS Lett. 591 (1) 155-163 [2017-01-00; online 2016-12-20]

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.

Affiliated researcher

PubMed 27925654

DOI 10.1002/1873-3468.12504

Crossref 10.1002/1873-3468.12504


Publications 7.1.2