Fig. 5: Localized chaperone effects on folding of a multi-domain protein. | Nature Communications

Fig. 5: Localized chaperone effects on folding of a multi-domain protein.

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

Fig. 5

a The six-domain EF4 protein exhibits multiple AP score peaks (gray line), indicating several locations of co-translational folding. The vertical gray bar indicates the position of full-length protein extrusion from the ribosome. Chaperone deletions (Δchaperone scores for \(\Delta\) tig, gold, and \(\Delta\) dnaKJ, blue) result in localized changes with both positive and negative signs. b Δchaperone scores mapped onto the native structure of full-length EF4. Trigger factor deletion elicits large effects on co-translational folding, most prominently for the G-domain and domain III. c Comparison of Δchaperone scores for trigger factor and DnaK. Trigger factor causes larger changes to co-translational folding than DnaK. d Trigger factor causes opposite effects on neighboring alpha-helix and beta-sheet. Source data are provided as a Source Data file.

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