Fig. 1
From: Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF
MLL4-PHD6 recognizes the histone mark H4K16ac. a Schematic of the MLL4 complex. b MLL4 domain architecture. c Superimposed 1H,15N heteronuclear single quantum coherence (HSQC) spectra of MLL4-PHD61503–1562 collected upon titration with H41–23, H41–9, and H412–23 peptides. Spectra are color coded according to the protein:peptide molar ratio. See also Supplementary Fig. 1, first panel. d Superimposed 1H,15N HSQC spectra of MLL4-PHD61503–1562 collected upon titration with H4K16ac1–23 peptide. Spectra are color coded according to the protein:peptide molar ratio. e Representative binding curves used to determine the Kd values by fluorescence spectroscopy (also see Supplementary Fig. 5). f Binding affinities of wild-type MLL4-PHD6 for the indicated histone peptides measured by tryptophan fluorescence. Error represents s.d. in triplicate measurements. Source data are provided as a Source Data file. g Binding curves used to determine the Kd values by microscale thermophoresis. Error represents s.d. in triplicate measurements. h A schematic showing specific reading of the H4K16ac mark by MLL4-PHD6
