Roles of Protein Synthesis Elongation Factor EF-Tu in Heat Tolerance in Plants
Figure 3
Proposed chaperone-like activity of EF-Tu in plant abiotic stress response. Abiotic stresses can affect protein native conformation and cause protein unfolding (denaturation). Unfolded forms are characterized by exposed hydrophobic residues which promote protein hydrophobic interactions and formation of protein aggregates. Protein denaturation due to stress is reversible unless followed by aggregation. (a) Denatured proteins form aggregates without chaperones, for example, EF-Tu, present. (b) EF-Tu binds to the exposed hydrophobic residues, prevents protein aggregation, and facilitates proteins to return to their native conformation when conditions return normal. In a manner similar to small HSPs, EF-Tu does not require presence of other chaperones or GTP (ATP) for chaperone activity.
