Fig. 2: Structural basis for binding of MORFWH2 to DNA.
From: MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix ___domain
a Confocal images of GST-MORFWH2 or GST (control) bound to glutathione Sepharose beads in the presence of FAM-labeled 37 bp dsDNA. Scale bar, 20 µm. b Overlay of 1H,15N HSQC spectra of MORFWH2 in the presence of increasing amount of 15 bp A-rich dsDNA (A-DNA15). Spectra are color coded according to the protein:DNA molar ratio. c Histogram of normalized CSPs in 1H,15N HSQC spectra of MORFWH2 induced by a fourfold molar excess of A-DNA15 as a function of residue. d–f The solution NMR structure of MORFWH2. Residues of MORFWH2 that exhibited large CSPs upon addition of A-DNA15 (greater than average plus one standard deviation, indicated by the dotted line in c) are mapped on the structure of MORFWH2, colored orange and labeled in d. Electrostatic surface potential of MORFWH2, with blue and red colors representing positive and negative charges, respectively, is shown in e. Two positively charged regions of MORFWH2 are indicated by green dotted ovals, with lysine and arginine residues labeled. Ribbon diagram of the MORFWH2 structure in the same orientation as in d and e is shown in f. Lysine and arginine residues of the two positively charged regions are shown in sticks and labeled. g EMSA of 147 bp 601 DNA in the presence of increasing amounts of K127A/K131A MORFWH2 and R151A/R153A/K157A/R158A MORFWH2 mutants. DNA:protein ratio is shown below the gel images. Source data are provided as a Source Data file.
