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. Author manuscript; available in PMC: 2010 Jan 10.
Published in final edited form as: Cell. 2009 Jul 10;138(1):63–77. doi: 10.1016/j.cell.2009.06.030

Figure 2. Structural anatomy of the human SLX4 complex.

Figure 2

(A) Summary of the interaction data showing the approximate location of binding between SLX4 and associated proteins.

(B) DN-Score versus Z-Score plots for HA-SLX4ΔN and HA-SLX4ΔC showing the identity of proteins identified by mass spectrometry (see Figure 1 legend for details).

(C) Summary of proteomic data for HA-SLX4ΔN, HA-SLX4ΔC, and HA-SLX4SBD. TSC, total spectral counts. The full list of interacting proteins is provided in Table S1.

(D–F) Domain mapping of SLX4 and its associated proteins. The indicated MYC-tagged proteins were expressed in 293T cells, immunoprecpitated as indicated, and immunoblotted. α-CDK2; loading control.

(G, H) Interaction of SLX4 with target proteins using the yeast two-hybrid system. The indicated proteins were cloned into activation domain (AD) or DNA-binding domain (DB) vectors and two-hybrid analysis performed as described under Experimental Procedures.

(I) Sequence relationship between vertebrate, yeast, Drosophila and C. elegans SLX4 in the C-terminal region involved in binding SLX1.