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. Author manuscript; available in PMC: 2013 Feb 1.
Published in final edited form as: Mol Microbiol. 2012 Jan 4;83(3):565–578. doi: 10.1111/j.1365-2958.2011.07951.x

Figure 1. TbKIN-C possesses in vitro ATPase activity and associates with tubulin microtubules in vivo.

Figure 1

(A). In vitro ATPase activity assay of the motor domain of TbKIN-C. The motor domain of TbKIN-C (MDTbKIN-C) and its K196A mutant (MD-KATbKIN-C) were purified as GST-fusion proteins from E. coli (left panel) and used for in vitro ATPase assays (right panel). Purified GST protein was included as a control. (B). In vivo association of TbKIN-C with tubulin microtubules in trypanosomes. 3HA-tagged TbKIN-C in soluble fraction and insoluble cytoskeleton fraction of trypanosome cells were detected by Western blot with anti-HA antibody. The same blot was also probed with anti-α-tubulin antibody and anti-α6 protein, a subunit of the 26S proteasome. S: supernatant; P: pellet.