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Current Biology, Volume 21 Supplemental Information
Deciphering Histone Posttranslational Modification Codes using Peptide Arrays Stephen M. Fuchs, Krzysztof Krajewski, Richard W. Baker, Victoria L. Miller, and Brian D. Strahl
H3K4me0
H3K4me1
H3K4me2
H3K4me3
H3K9me
H3K18me H3K18me/ K36me H3K36me
H3K79me
H2A
H2B
H4
e3 39 a αH c/S1 0 3S 10 pho ph s os αH 3K 14 ac αH 3K αH 79 3K me 79 1 m e2 αH 3K 79 m e3 αH 4K 5a c/ K8 ac /K 12 ac /K 16 ac
Figure S1. Heat map of all experimental antibody data. Data was normalized to the strongest interaction plotted on a scale from 0 to 1 with 1 (yellow) being the most significant. Figure S2. Comparison of H3K4 methyllysine-specific antibodies for different methylation states (H3K4me1 – Millipore 07-436, H3K4me2 – Active Motif 39142, H3K4me3 – Active Motif 39160). Data are plotted as the mean with SEM for the indicated peptide from a single array. The results of two independent arrays are shown. Differences in intensities were compared using two-way ANOVA analyses and confidence intervals (* 95% and *** 99.9%) are indicated for individual comparisons. Figure S3. Effect of neighboring acetylation on BPTF binding. Data are plotted as the mean with SEM for the indicated peptide from a single array. Differences in intensities were compared using two-way ANOVA analyses and confidence intervals (* 95%, ** 99% and *** 99.9%) are indicated for comparisons to the H3K4me3 peptide with no other modifications (left). Figure S4. Scatter plots comparing two arrays for RAG2, BPTF, and CHD1.
Each peptide was printed as a series of 6 sequential spots on each of four subarrays. The layout of subarrays 1 and 3, and 2 and 4 are identical. Parentheses denote the location within a subarray where a given peptide was printed.
