Fig. 1: Arrest peptide-mediated detection of co-translational folding in cells. | Nature Communications

Fig. 1: Arrest peptide-mediated detection of co-translational folding in cells.

From: Arrest Peptide Profiling resolves co-translational folding pathways and chaperone interactions in vivo

Fig. 1

a Co-translational folding near the ribosome surface generates force and resumes translation arrested by the SecM arrest peptide (AP). b The candidate protein is fused to the SecM AP and GFP. Candidate folding results in increased GFP synthesis. The coding sequence of mCherry under control of a separate promoter on the same plasmid serves as an internal control. c Cytometry results of the individual reporter constructs. A non-folding truncation of EF-G (ncodons = 212) shows low GFP signal, whereas a variant for which stable folding is expected (ncodons = 331) shows medium to high GFP signals. An arrest-defective AP variant (APmut) shows even higher GFP signal, delineating the upper boundary of the reporter readout. d Histogram of the GFP and mCherry signal ratios from the different variants. Imposing boundaries along constant log10(GFP/mCherry) ratios illustrates how the distribution of reporter signal can be reconstructed from cell sorting counts. Source data are provided as a Source Data file.

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