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. 2012 Jun 15;125(12):2954–2964. doi: 10.1242/jcs.101592

Fig. 4.

Fig. 4.

H2A.Z is associated with H3 K4me3 in mammalian cells. (A–D) MDA-MB-468 cells were fixed with methanol:acetic acid and incubated with anti-H3 K4me3–Alexa-Fluor-488 antibodies only (donor) (A), with anti-H3 K4me3–Alexa-Fluor-488 plus anti-H2A.Z–Alexa-Fluor-647 antibodies (donor and acceptor in left and right panels, respectively) (B), with anti-H3 K36me3–Alexa-Fluor-488 antibodies only (donor) (C) or with anti-H3 K36me3–Alexa-Fluor-488 plus anti-H2A.Z–Alexa-Fluor-647 antibodies (donor and acceptor in left and right panels, respectively) (D), and then analyzed by FLIM-FRET. (E) Fluorescence lifetime distribution of samples shown in A–D. (F) Sequence alignments between yeast and human H2A and Hta1p/H2A.Z are shown. Ten amino acid intervals on H2A and Htz1p/H2A.Z are noted by filled and open circles, respectively. Mutation of residues highlighted in red in yeast H2A result in defects in H3 K36me3 by Set2p. The docking domain is shown with a solid line. (G,H) Composition of nucleosomes containing the histone variants. Scale bars: 10 µm. FLIM scale: 0 nanoseconds, blue; 3.9 nanoseconds, red. See also Table 1.