Fig. 7.
Bivalent binding of AF9-YEATS is not conserved in Taf14-YEATS. a EMSA with 5 pmol/lane 20 bp dsDNA incubated with increasing amounts of AF9-YEATS. b Binding curves used to determine Kd for the DNA:AF9-YEATS complex by EMSA. The band of free DNA was used for quantification of the complex formation. Binding constants are obtained from duplicate measurements as mean ± standard error. c A schematic of the bivalent interaction of AF9-YEATS with histone H3K9cr and DNA. d Alignment of the YEATS domain sequences: absolutely, moderately, and weakly conserved residues are colored green, orange, and pink, respectively. Positively charged residues in three patches are indicated by blue boxes. The residues of AF9-YEATS mutated in this study are labeled. e Electrostatic surface potential of Taf14-YEATS in complex with the H3K9cr peptide. f EMSA with 1.88 pmol/lane 601 DNA and increasing concentration of Taf14-YEATS