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. 2012 Feb 20;7(2):e30738. doi: 10.1371/journal.pone.0030738

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Erent et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Klp5₄₃₆GST includes the motor domain, the putative coiled-coil domain [36], PreScission protease cleavage site and glutathione-S-transferase (GST) tag. Klp6₄₄₀His contains the motor domain, complete putative coiled-coil domain [36] and 6×His C-terminal tag. Klp6₄₁₅His contains the first 11 amino acids of the coiled coil domain and a 6His C-terminal tag. Predicted molecular weight of constructs are Klp5₄₃₆GST: 74.9 kDa, Klp6₄₄₀His: 50.2 kDa, Klp6₄₁₅His: 47.2 kDa and Klp5₄₃₆ after GST tag cleavage 48.5 kDa. (B) Colloidal Coomassie stained SDS-PAGE of desalted Klp6₄₁₅His, microtubule affinity-purified Klp6₄₄₀His; microtubule affinity-purified Klp5₄₃₆GST and Klp5₄₃₆ (Klp5₄₃₆GST after PreScission protease cleavage and purification). (C) Klp6₄₄₀His forms a homodimer. Superimposed elution profiles of Superose 12 chromatography of Klp6₄₁₅His (blue), Klp6₄₄₀His (red) and a mixture of Klp6₄₁₅His and Klp6₄₄₀His (green). Elution profiles are consistent with monomeric Klp6₄₁₅His and homodimeric Klp6₄₄₀His. Elution positions of Ovalbumin (43 kDa) and Bovine Serum Albumin (67 kDa) are indicated. Arrowhead indicates the position of a larger complex present in the Klp6₄₄₀His sample.