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. 2015 Dec 10;10(12):e0144673. doi: 10.1371/journal.pone.0144673

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© 2015 Breit 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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Fig 2 — (A-C) Bub1^kinase and Bub1:Bub3 complex exhibit similar catalytic activity toward H2A (A) and Bor:Sur substrates (B) and hydrolyze ATP at similar rates (C). The mutation D917N abrogates ATPase activity (C). The kinase activity was determined using the ADP-Glo^TM Kinase Assay and is plotted as a function of substrate concentration to allow fitting according to the Michaelis-Menten equation with R² = 0.99 (Bub1^kinase on Bor:Sur R² = 0.97). KD–kinase dead. Error bars represent SD of a mean of at least 2 independent experiments. (D) Kinetic parameters of the Michaelis-Menten fits as determined in (A-C). (E) H2A contained in H3- or CENP-A nucleosomes is efficiently phosphorylated by Bub1^kinase and Bub1:Bub3. (F) The kinase activity, plotted as a function of substrate concentration, allows fitting with the Michaelis-Menten equation with R² = 0.95 (H3) and 0.99 (CENP-A). Error bars represent SD of a mean of at least two independent experiments. (G-H) EMSA assays showing DNA and nucleosome binding of Bub1^kinase and H3- or CENP-A nucleosomes. MN–mononucleosomes.