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. Author manuscript; available in PMC: 2019 Jan 11.
Published in final edited form as: Cell. 2017 Dec 28;172(1-2):331–343.e13. doi: 10.1016/j.cell.2017.12.008

Figure 1. Overview of the Ku-Tlc1KBS Complex Structure.

Figure 1

(A) Domain organization of S. cerevisiae TLC1, Ku70/80, and Sir4. Top: predicted secondary structure of TLC1. Conserved domains, motifs and interacting proteins are designated. TLC1KBS is denoted with a dashed box. Bottom: domain organization of Ku70/80 and Sir4. The shaded areas indicate the interactions of Ku70/80-TLC1, Ku70-Ku80 and Ku80-Sir4, respectively. (SID: Sir2-interacting domain; PAD: partitioning and anchoring domain; CC: coiled coil). (B) ITC measurement of the interaction between Ku70/80 and TLC1KBS. Inset: ITC titration data. (C) Two orthogonal views of the overall structure of the Ku-TLC1KBS complex. Ku70, Ku80 and TLC1KBS are colored in green, slate blue and orange, respectively. (D) Overall conformation of TLC1KBS in the Ku-TLC1KBS complex. The A292U293 and A304 bulges are colored in cyan.

See also Figure S1 and Table S1.