Skip to main content


Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Fig. 1 | Epigenetics & Chromatin

Fig. 1

From: Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions

Fig. 1

SPIN1 triple Tudor domain interacts with H4K20me3 as well as H3K4me3. a Heat map showing the relative binding detected for each of the indicated domains on the peptide microarray platform. Data represent the average of two independent arrays relative to the most intense binding signal within the indicated set of peptides. b Scatter plot of the relative binding of SPIN1 triple Tudor domain from two independent peptide arrays. H3K4me3-containing peptides are shown in red and H4K20me3-containing peptides are shown in blue. All other peptides are shown in black. c Representative picture of a section of the peptide microarray for SPIN1 triple Tudor domain. The left panel shows both the green (peptide) and red (protein binding) fluorescent channels, while the right panel depicts only the red fluorescence channel for clarity. Positive antibody controls are outlined in white and the positive interaction with the H4K20me3 peptide is outlined in yellow. Full array images are shown in Additional file 3: Figure S1. d Western blot results of peptide pull-down experiments with purified full-length Spindlin family members. The input is shown in Lane 1 and the corresponding bound fraction is shown in Lanes 28. e Western blot results of peptide pull-down experiments with whole cell lysates derived from transiently transfected HEK 293T cells (GFP-SPIN1, 2A, 2B, 3 and 4). f Western blot results of peptide pull-down experiments with purified SPIN1 wild type (SPIN1WT) or aromatic cage mutant in the second Tudor domain (SPIN1Y170A) demonstrating a loss of H3K4me3 and H4K20me3 in the mutant

Back to article page