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. Author manuscript; available in PMC: 2015 May 6.
Published in final edited form as: Structure. 2014 Mar 27;22(5):697–706. doi: 10.1016/j.str.2014.03.002

Figure 1. VtI997A and VtV1001A are deficient in F-actin binding and bundling yet retain association with PIP2.

Figure 1

(A) SDS-polyacrylamide gel electrophoresis of supernatant (S) and pellet (P) fractions after co-sedimentation of Vt with F-actin. Actin concentrations and Vt variants are noted. (B) Quantification of F-actin co-sedimentation assays identifies Vt variants in H4 deficient in F-actin binding. (C) Vt variants deficient in binding to F-actin are also defective in F-actin bundling. (D) VtV1001A, while deficient in actin binding, retains PIP2 binding comparable to VtWT. VtI997A is impaired in PIP2 binding. Error bars are standard deviation, n= 3. See also Figure S1.