Mutational analysis of protein folding inside the ribosome exit tunnel

作者：Farias Rico Jose Arcadio; Goetz Sara Kathrin; Marino Jacopo; von Heijne Gunnar^*

来源：FEBS LETTERS, 2017, 591(1): 155-163.

DOI：10.1002/1873-3468.12504

• arrest peptide
• cotranslational protein folding
• ribosome

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.

• 出版日期2017-1