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. 1998 Nov 2;143(3):673–685. doi: 10.1083/jcb.143.3.673

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Biochemical analysis of Xklp2 cosedimentation with microtubules. Taxol (1 μM) and the m70.1 antibody (1–2 mg/ml) were added as indicated to 150,000 g egg extracts and the reactions incubated for 30 min at 20°C. M, mitotic extract, I, interphase extract. Microtubule pellets (corresponding to 5 μl of extract) and soluble fractions (corresponding to 0.25 μl of extract) were analyzed on Coomassie-stained gels and Western blots probed for the proteins indicated (DIC, dynein intermediate chain). (A) Sedimentation of endogenous Xklp2. (B) Sedimentation when either GST-Xklp2-Tail, T, or GST-Xklp2-LtoK, K, were added to the extract at 0.3 μM. Xklp2 as well as the GST-Xklp2-Tail sediment with microtubules in a mitotic cytoplasm. GST-Xklp2-Tail (52 kD) runs very close to the tubulin doublet. This is why the band on the Western blot of the microtubule pellet appears broadened. Also the dynein intermediate chain is enriched in mitotic microtubule pellets. When the m70.1 antibody is added the dynein intermediate chain is not associated with microtubules anymore and the binding of Xklp2 and GST-Xklp2-Tail to microtubules is reduced. The molecular mass of marker proteins is indicated on the right.