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. 2017 Apr 3;216(4):961–981. doi: 10.1083/jcb.201611060

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© 2017 Mosalaganti et al.

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Figure 6. — RZZ interaction with Spindly is direct and requires farnesylation. (A) Elution profiles and SDS-PAGE analysis of SEC experiments with the indicated proteins. The elution volume of the RZZ–Spindly complex after treatment with FTase and Fpp as substrate shifts significantly, whereas farnesylated Spindly (Spindly^Farn) elutes like unmodified Spindly. (B) Summary of XL-MS data reporting ROD–Spindly intersubunit cross-links. (C) Sedimentation velocity AUC profiles of recombinant mCherry-Spindly. The calculated molecular mass for a complex containing two copies of each subunit is shown. (D) Sedimentation velocity AUC profiles of the RZZ–Spindly^Farn complex. The calculated molecular mass for a complex containing two copies of each subunit is shown. (E–G) Sedimentation velocity AUC profiles of the RZZ–mCherry–Spindly^Farn at 5, 10, and 15 µM. “Mass (app)” denotes the apparent mass of RZZ derived from the velocity runs; “s” denotes the sedimentation coefficient; “Frict. ratio” is the frictional ratio of the Spindly particle. In E, the calculated molecular mass for a complex containing two copies of each subunit is shown. AU, arbitrary units.