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. Author manuscript; available in PMC: 2012 Oct 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Jul 19;1809(10):557–566. doi: 10.1016/j.bbagrm.2011.07.004

Figure 2. The Hpc2 C-terminal region is essential for HIR complex assembly.

Figure 2

(A) Schematic of the wild-type Hpc2 protein with three conserved domain CDI, CDII and CDIII. (B) Whole cell extracts was made from the indicated strains, YPP461, YPP463, and YPP492, containing different TAP tag and Myc tag HIR subunits and deleted of the endogenous HPC2, as indicated, and transformed with the indicated HPC2-HA tag YCp:URA3 plasmid: WT, wild-type HPC2; −, empty plasmid; ΔC, HPC2ΔC-548 mutant; ΔN, HPC2ΔN-150 mutant. Co-immunoprecipitation assays were performed using IgG-sepharose beads and analyzed by Western blotting with anti-HA (to probe for Hpc2-HA), anti-Myc (to probe for the indicated Myc tag proteins), and peroxidase anti-peroxidase (α-PAP) (to probe for indicated TAP tag subunit) antibodies. The asterisks correspond to the TAP tagged proteins signal revealed by the HRP-couple secondary antibody used for the anti-Myc Western blot. (C) Same as (B) except that YPP996 (HIR2-TAP hpc2::KANMX6) strain was used and transformed with indicated YIp:TRP1 plasmid encoding the indicated forms of HPC2 wild-type (WT) and mutants.