Figure 6. A model for co-translational stress response via early ribosome pausing.

The cytosolic chaperone molecules, such as Hsc70 (green), not only assist the co-translational folding, but also facilitate the elongation of emerging polypeptides (red). Under the condition of proteotoxic stress, the accumulation of misfolded proteins titrates out molecular chaperones. The lack of co-translational interaction of chaperone molecules leads to early elongation pausing and rapid suppression of global protein synthesis.