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Figure 2.
Characterization of the Eaf3 chromo domain binding to histone
H3 peptides. A, characterization of binding of the Eaf3 chromo
domain with various histone H3 peptides using isothermal
titration calorimetry: H3K36me3 peptide (a); H3K36me2 peptide
(b); H3K36 peptide (c); H3K4me3 peptide (d); H3K4me2 peptide
(e); H3K9me3 peptide (f). The upper panels show the raw data for
injections of the peptides into the Eaf3 chromo domain, and the
lower panels show the integrated heats of the injections. B,
binding of the short form Eaf3 chromo domain with the H3K36me3
peptide measured by ITC and SPR. C, binding of the long form
Eaf3 chromo domain with the H3K36me3 peptide measured by ITC and
SPR. RU, response units. D, binding of the wild-type and mutant
Eaf3 chromo domain with the H3K36me2 peptide using in vitro
binding assay. Negative control 1 (N1) shows that the H3K36me2
peptide does not have nonspecific binding with the nickel beads;
negative control 2 (N2) shows that the Eaf3 chromo domain does
not have nonspecific reaction with the anti-H3K36me2 antibody;
positive control (P) shows the specific binding between the
H3K36me2 peptide and the anti-H3K36me2 antibody.
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