Fig. 2: The KJE chaperone system accelerates FLuc folding. | Nature Communications

Fig. 2: The KJE chaperone system accelerates FLuc folding.

From: Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein

Fig. 2: The KJE chaperone system accelerates FLuc folding.

a Structure of FLuc (PDB ID: 1LCI) with domains indicated. b Spontaneous and chaperone-assisted folding of 100 nM FLuc was assayed upon dilution from 5 M GuHCl into buffer without or with KJE-ATP, respectively, by monitoring luminescence activity. KJE-mediated folding was performed with 3 µM DnaK, 1 µM DnaJ, 1.5 µM GrpE and 5 mM ATP. Error bars represent s.d. (n = 10). c Concentration dependence of FLuc refolding. FLuc was diluted from denaturant to different final concentrations (0.1–200 nM) and refolding assayed as in (b). Rescue of spontaneous folding reactions was assayed by adding KJE-ATP (0.3 µM DnaK, 0.1 µM DnaJ, 0.5 µM GrpE and 5 mM ATP) after 2, 4 or 8 h. Error bars represent s.d. (n = 3). Ass., KJE-ATP-assisted; Spont., spontaneous folding. Source data are provided as a Source Data file.

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