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Figure 3


Fig. 3. Interaction of the N-terminal region of obscurin/Obsl1 with titin. (A) Sub-mapping of the minimal binding domain of obscurin/Obsl1 to titin M10 and of titin to obscurin/Obsl1 Ig1 by Y2H assays identified that Ig1 of obscurin/Obsl1 (top) and M10 of titin (bottom) are sufficient for the binding. (B) These interactions were also verified by pulldown assays using GST-M10 bound to glutathione beads and GFP-tagged obscurin/Obsl1 Ig1 constructs. Detection was performed by blotting equivalent amounts of input (I), unbound (U) and bound (P) fractions with anti-GFP antibody. (C) Ternary-complex formation between obscurin, titin and myomesin in pulldown assays. GST–titin-M10 beads were incubated with GFP–My4-My5 alone (left) and in the presence of obscurin Ob-Ig1-Ig2 (middle) or Ob-Ig1-Ig3 (right). Ob-Ig1-Ig2 binds to titin M10, but myomesin My4-My5 is only bound when the binding site on Ob3 is present, demonstrating the formation of a ternary complex by independent binding motifs.





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