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. 2021 Feb 9;53(2):250–263. doi: 10.1038/s12276-021-00564-4

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© The Author(s) 2021

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Fig. 5 — a Synthetic peptides were used in this study to determine methylated lysine residues. b Only peptide #2, spanning amino acids 153–167 in the MADS-box of SRF, was methylated by GST-SET7. SRF synthetic peptides were used as substrates and incubated with GST-SET7 in the in vitro methyltransferase assay. c To determine the critical lysine, K154-, K165-, and K165A-bearing SRF synthetic peptides were generated and used in the in vitro methyltransferase assay. SRF K154 did not show any methylation, whereas SRF K165 emitted a strong methylation signal. Notably, SRF K165A showed one-half the methylation as the WT peptide, which suggested methylation of other lysine residues in addition to SRF K165. d GST-SRF WT, GST-SRF K154A, GST-SRF K165A, and GST-SRF K154/165A were used in the in vitro methyltransferase assay. For the methylation enzyme, GST-SET7 was supplemented. Notably, the methylation was nearly completely abolished when both K154 and K165 were substituted with alanine, which suggests that both SRF K154 and K165 are methylated by SET7. *p < 0.05; ** and ^@@p < 0.01; NS, not significant.