Extended Data Fig. 5: Chaperoning of TA clients by Sgt2’s disordered tail.

a, ITC analysis of Sec22^TMD-loaded Sgt2 binding to Get4/5 highlights the interaction potential induced by client loading. b, ITC analysis of Sgt2-Tau^fragment and Get4/5 shows no interaction, indicating that the non-relevant Tau fragment fails to promote Sgt2-Get4/5 binding. c. Methyl-TROSY NMR spectra comparison of Sgt2^FL (gray) and Sgt2-Ysy6^TMD (rose red) reveals signal broadening in Sgt2^C upon client binding, indicating the involvement of Sgt2’s C-terminal tail in chaperoning the TA client Ysy6. d-e, Differential line broadening analysis identifies binding sites within Sgt2^C for Ysy6T^MD (d) and Sec22^TMD (e), pinpointing residues involved in chaperoning. The overlap in these sites suggests a universal chaperoning mechanism for different TA clients. f, Sgt2 amino acid sequence highlighting domains and TA client binding site. g, Hydrophobicity plot of Sgt2^C as a function of its primary sequence, with the TA client binding site annotation. The alignment of regions with high hydrophobicity score and the binding site indicates that Sgt2^C likely uses its hydrophobic area to chaperone TA clients’ transmembrane domains.