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. 2014 Feb 18;9(2):e89399. doi: 10.1371/journal.pone.0089399

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© 2014 Makrantoni 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) Coomassie-stained gel showing recombinant GST-Sli15-His₆ preparations used for in vitro phosphorylation and microtubule binding. (B) Phosphorylation of GST-Dam1 by Ipl1 in the absence or presence of wild-type (Sli15) or mutant forms (Sli15-20A, Sli15-20D) of GST-Sli15-His₆. Top panel, GST-Sli15-His₆ phosphorylation (³²P incorporation from [γ-³²P]ATP); middle panel, GST-Dam1 phosphorylation (³²P incorporation from [γ-³²P]ATP); lower panel, GST-Dam1 detected by Coomassie staining. (C) Phosphorylation of H3.3 by Ipl1 in the absence or presence of wild-type or mutant forms of GST-Sli15-His₆. Top panel, GST-Sli15-His₆ phosphorylation (³²P incorporation from [γ-³²P]ATP); middle panel, H3.3 phosphorylation (³²P incorporation from [γ-³²P]ATP); lower panel, H3.3 detected by Coomassie staining. The histograms show mean relative specific activity (n = 3) of H3.3 (B) and GST-Dam1 (C) phosphorylation by Ipl1 promoted by GST-Sli15-20A-His₆ or GST-Sli15-20D-His₆ in comparison with GST-Sli15-His₆ (arbitrarily set to 1.0).