Figure 4 | Scientific Reports

Figure 4

From: Effects of charge-modifying mutations in histone H2A α3-domain on nucleosome stability assessed by single-pair FRET and MD simulations

Figure 4

Salt-induced nucleosome disassembly monitored by various labeling strategies in microplate-scanning FRET experiments. (a) Representative representation of normalized average proximity ratio as a function of NaCl concentration for wild type (top) and mutated (bottom) nucleosomes with different labeling strategies. Black circles: IβIα nucleosomes, Red squares: H2B-Iα nucleosomes, Green triangles: H2B-Dyα nucleosomes, Lines: Sigmoidal fit. (b) Averaged c(1/2)-values and standard error of the mean (calculated from three independent replicas) for all constructs, revealing a decrease in overall stability of nucleosomes and changes of the nucleosome opening sequence with mutations. RE-mutants are less stable than the respective RA-mutants and show an altered nucleosome opening sequence. The effect of RA-mutations depends on the position of the introduced amino acid (R88A < R81A < R81A/R88A), but the nucleosome opening pathway is comparable to wild type nucleosomes.

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