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. 2016 Jul 6;113(29):E4151–E4160. doi: 10.1073/pnas.1605951113

Fig. 8.

Fig. 8.

Model for interactions between Ltn1 and Rqc2. (A) Schematic representation of the interaction of yeast Ltn1 (salmon) with a model of yeast Rqc2 (green) and the SRL. The EM map of the yeast RQC (EMD-6170) contoured to 1.5σ is displayed in blue showing the fit of the proteins in the maps. (B and C) Comparison of the Ltn1-Rqc2 interface and the Ltn1 N termini in yeast versus mammals. (B) Schematic representation of yeast Ltn1 (salmon) and Rqc2 (green). The EM map of the yeast RQC contoured to 1.5σ is displayed in blue, and Ltn1 residues 14–35 are colored red, highlighting the presence of electron density for this region. The position of the extreme N-terminal helix (orange) of the human Ltn1 NTD based on an alignment with the yeast RQC is indicated by an arrow demonstrating the lack of electron density in this region of the map. (C) Schematic representation of the human Ltn1 (orange) and Rqc2 (teal) interface (PDB ID code 3J92) with the EM map from the mammalian RQC (EMD-2832) contoured at 1.5σ. The position of the extreme N terminus from yeast Ltn1 is shown in red, and the human Ltn1 extreme N terminus is indicated by an arrow. (D) Secondary structure-based sequence alignment of the N-terminal residues from yeast and metazoans. Conserved residues are highlighted in black (highly conserved) and gray (moderately conserved). The secondary structure of yeast Ltn1 is shown above the sequence alignment whereas that of the human structure is shown below. Ltn1 residues in the interface with Rqc2 in yeast are indicated by pink dots above the residues.