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. 2019 Sep 20;9:13613. doi: 10.1038/s41598-019-49894-4

Figure 5.

Figure 5

Analysis of labeling incorporation of multiply modified histone proteins. (A) Relative labeling incorporation at day 1–3 of the two peptides of histone H3 with the largest number of combinatorial isoforms, KSTGGKAPR (aa 9–17) and KSAPATGGVKKPHR (aa 27–40). Highlighted in red, peptide carrying both flanking modifications. P-value is calculated as paired t-test across the three days. All data were extracted after 2 days of labeling. All significance estimations are based on a two-tail heteroscedastic t-test (significant when p-value < 0.05). (B) Same representation for all the modified states of the peptide GKGGKGLGKGGAKR of histone H4, containing all the amino acid residues with the highest amount of acetylation. (C) Example of co-existing acetylations on the peptide of histone H3 KQLATKAAR (aa 18–26). The doubly acetylated form has higher labeling incorporation rate. (D) Relative incorporation of heavy labeled histidine of the differently modified forms of histone H3 N-terminal tails.