Figure 1
From: Binding to medium and long chain fatty acyls is a common property of HEAT and ARM repeat modules
Identification of the binding candidates of protein acyl modifications. (a) SILAC (Stable Isotope Labeling by/with Amino acids in Cell culture) and peptide pull-down experiment design. Each pair of peptide pull-downs were repeated twice, through forward (unmodified-light, acyl-heavy) and reverse (unmodified-heavy, acyl-light) experiments. (b) Structures of unmodified (unmod) and acyl-modified lysine side chain of the peptides used in this study. (c and d) Scatter plots showing protein quantification results of forward (x-axis) and reverse (y-axis) experiments for two lysine myristoylated peptides compared with the corresponding unmodified peptide. Red dots highlight proteins with HEAT or ARM repeats. The large orange dot on the upper right corner of (c,d) represents proteins (42 in H3K27myr experiment; 37 in H3K9myr) with no forward and reverse ratios reported by MaxQuant software but manually found enriched based on peptide signals, among which 23 and 14 proteins are HEAT or ARM repeat proteins respectively.
