Figure 4. Effect of TF dimerization on chaperone activities.

Aggregation of GAPDH in the absence or presence of TF and TF^mon at 0.5 μM (A) and OmpA in the absence or presence of TF and TF^mon at 4 μM (B). (C) Refolding of MBP in the absence or presence of TF and TF^mon. The solid line represents the fit of the data to a single exponential function. (D) Folding rates of MBP from the analysis of the curves shown in panel C. (E) Refolding of the slowly-folding MBPY283D variant in the absence or presence of TF and TF^mon.

Figure 4—figure supplement 1. Aggregation of GAPDH in the absence or presence of 1 µM TF and TF^mon.

The aggregation of GAPDH was monitored by 90° light scattering at 620 nm.

Figure 4—figure supplement 2. Sequence hydrophobicity of the substrate proteins of TF (Roseman algorithm, window = 9).

(A) Hydrophobicity plot of PhoA as a function of its primary sequence. TF-binding sites determined by NMR (Saio et al., 2014) are highlighted in green. (B) Hydrophobicity plot of GAPDH (left panel) and OmpA^1-192 (right panel) as a function of their primary sequences. The hydrophobic stretches that are expected to bind to TF are highlighted in light blue.