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. Author manuscript; available in PMC: 2010 Sep 26.
Published in final edited form as: Mol Cell. 2010 Mar 26;37(6):834–842. doi: 10.1016/j.molcel.2010.01.037

Figure 4. Nap1 disfavors the interaction between H2A–H2B dimer and DNA.

Figure 4

The experimental design for each reaction is shown above each panel, using the symbols described in Fig. 1. Fluorescent labels are indicated by asterisks; FRET is indicated by a red arrow. Closed squares are 601-tetrasomes; closed triangles are 5S-tetrasomes. (A) Normalized fluorescence as a function of DNA binding to H2A–H2B. (B) The change in FRET between Nap1 and H2B as a function of DNA. The experiment was originally designed to confirm K6; however, the data indicate the Nap1-H2A–H2B complex remains intact in the presence of DNA and thus the small amount of signal change is due to DNA binding to the Nap1-H2A–H2B complex. Therefore, the binding event really monitored is K5, and is thus termed K5*. (C) Fluorescence change as a function of DNA binding to a Nap1-H2A–H2B complex (Nap1 is 10-fold > K2). Binding constants derived from the shown experiments are summarized in Table 1. See supplemental information for experimental details.