Fig. 7

Speculative schematic representation of the hydrophobic substrate recognition of SGTA. SGTA is well known to form a tight dimer through its N-terminal domain. Here, we discovered that the C-terminal region also dimerizes in a more transient or weak fashion, facilitating the capture and/or shielding of hydrophobic substrates such as the transmembrane helices of tail-anchored proteins. The structural arrangement of this C-terminal dimer and its mechanism of hydrophobic substrate binding are still a mystery and constitute an open field for further research