Structural insights into the interaction of the nuclear exosome helicase Mtr4 with the preribosomal protein Nop53

Biophysical characterization of Mtr4 binding to AIM-containing proteins. (A) Schematic representation of the domain structure of yeast Mtr4 and Nop53. Predicted unstructured regions are represented as gray lines. The Nop53 fragment identified by proteolysis contains the arch-interacting motif (AIM) identified by Thoms et al. (2015). (B) ITC experiments of Mtr4-ΔN with Nop53_prot and Utp18_prot. The open circles show the titration of Nop53_prot/Utp18_prot into the Mtr4-ΔN containing cell. The filled circles show the control where Nop53_prot/Utp18_prot were titrated into buffer. In each inset is the number of calculated binding sites (N), and dissociation constants (K_d) are shown.