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. Author manuscript; available in PMC: 2010 Nov 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Jan 25;1799(5-6):480–486. doi: 10.1016/j.bbagrm.2010.01.009

Figure 1. Nucleosomes reconstituted with H3K56Q and K56E.

Figure 1

A) Mutation of H3K56 to Q or E results in reduced electrophoretic mobility on triton-urea gels. 4 μg of refolded histone octamers containing mutations to histone H3K56Q (lane 1), H3K56Q with WT H3 (lane 2), WT (lane 3) and H3K56E (lane 4) were loaded and electrophoresed on an AU-PAGE gel stained with coomassie blue. (*) indicates wild type H3 and (**) indicates H3K56Q and H3K56E mobility. B) Reconstituted nucleosomes containing H3-K56 mutations have a similar ability to heat shift. Nucleosomes containing H3 K56Q (lanes 1 and 2), WT H3 (lane 3 and 4) and H3 K56E (lane 5 and 6) reconstituted with 147 bp α-Sat DNA. Nucleosomes were heat shifted (+) for 1 hour at 37°C (lanes 2, 4 and 6). Samples were separated on a 5 % native polyacrylamide gel and stained with ethidium bromide (top) and Imperial Protein Stain (Pierce) (bottom). M indicates 100 bp marker.

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