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Figure 1. CAF-1 binds H3-H4 with ∼20-fold higher affinity than H2A-H2B. Titration of CAF-1 into fluorescently labeled histone complexes (H3-H4 and H2A-H2B) results in a change in fluorescent signal, indicating direct binding events. The normalized fluorescent change was plotted against increasing CAF-1 concentration (log [CAF-1]) to produce a binding curve where the CAF-1 concentration at 50% fluorescent change equals the apparent dissociation constant (Kdapp) for the CAF-1/histone complex. CAF-1 binds H3-H4 in the low nanomolar range with the averaged data points shown as black circles. The data points were fit with a non-linear regression curve to establish the apparent dissociation constant and Hill coefficient. CAF-1 binds H2A-H2B with significantly lower affinity, which is seen by a rightward shifted binding curve (gray squares). The error bars represent the standard error within individual data points. The total data points for a single experiment are 48. Image published in: Winkler DD et al. (2012) © The Author(s) 2012. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license Larger Image Printer Friendly View

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