Table 3.
MBD interacts with the lysine-trimethylated H3 variants
K a (M−1) | K d (μM) | ΔH (kcal/mol) | ||
---|---|---|---|---|
MBD | H3 | 2.0 × 107 | 0.050 | –19.0 |
H3 K4me3 | 8.4 × 106 | 0.12 | –4.1 | |
H3 K9me3 | 1.3 × 107 | 0.075 | –59.0 | |
H3 K27me3 | 1.7 × 105 | 5.9 | 7.0 | |
H3 K36me3 | 3.3 × 105 | 3.1 | 4.0 | |
MBD R106W | H3 | 1.9 × 107 | 0.052 | –18.1 |
H3 K4me3 | 3.2 × 106 | 0.32 | –15.5 | |
H3 K9me3 | 2.0 × 107 | 0.051 | –51.9 | |
H3 K27me3 | 1.6 × 105 | 6.2 | 15.3 | |
H3 K36me3 | 6.1 × 104 | 16 | 7.7 | |
MBD R133C | H3 | 2.5 × 107 | 0.040 | –26.2 |
H3 K4me3 | 3.5 × 106 | 0.29 | –12.8 | |
H3 K9me3 | 2.2 × 107 | 0.046 | –51.1 | |
H3 K27me3 | 1.3 × 105 | 7.9 | 10.7 | |
H3 K36me3 | 6.7 × 105 | 1.5 | –3.7 |
Binding parameters for MBD (WT and Rett-associated variants) interacting with H3 trimethylated at K4, K9, K27 and K36 at pH 7, 20°C.