Fig. 3: DNA binding activity of Taf14_Linker.

a Overlay of ¹H¹⁵,N HSQC spectra of Taf14_FL in the presence of increasing amount of 147 bp 601 DNA. Spectra are color coded according to the protein:DNA molar ratio. b–e EMSAs of 147 bp 601 DNA in the presence of increasing amounts of the indicated GST-Taf14 proteins. DNA:protein ratio is shown below gel images. Images are from single experiment. Architecture of each Taf14 construct is depicted above the gels, and mutations are indicated with a blue asterisk. f, g Superimposed ¹H¹⁵,N HSQC spectra of the indicated Taf14 proteins collected upon titration with 147 bp 601 DNA (f) or Taf2_Linker g. Spectra are colored according to the protein:ligand molar ratio. h MST binding curves for the Taf2_Linker interaction with Taf14_ET. The K_d value represents average of two independent measurements, and error represents the standard deviation. n = 2 i, j Mass spectrometry analysis wheel diagram showing positions of DSSO-generated cross-links identified in the Taf14_FL (i) or Taf14_FL + 37 bp dsDNA j. Line thickness relates to the number of cross-link identifications. Taf14 domains within the circle are colored as in Fig. 1a. k Dimentionless Kratky plots of SAXS analysis for the indicated samples: Taf14_FL (blue), Taf14_FL + Taf2_CT (orange), or Taf14_FL + 37 bp dsDNA (green). l A model of the conformational rearrangement in Taf14_FL upon binding to DNA. m Overlay of ¹H¹⁵,N HSQC spectra of Taf14_FL in the presence of increasing amounts of H3K9cr_1-19 peptide. Spectra are colored according to the protein:peptide molar ratio. Source data are provided in a Source Data file.