Extended Data Fig. 8: Behavior of full-length GAF depends on multimerization by POZ domain. | Nature Structural & Molecular Biology

Extended Data Fig. 8: Behavior of full-length GAF depends on multimerization by POZ domain.

From: GAGA zinc finger transcription factor searches chromatin by 1D–3D facilitated diffusion

Extended Data Fig. 8

a, Representative kymographs show AF546-GAF-ΔPOZ binding to DNA over time on + hsp70 DNA. b, Representative fluorescence intensity trace for GAF-ΔPOZ showing an abrupt loss of fluorescence signal at 5.7 s due to either dissociation or photobleaching. c, Representative trace showing GAF-FL photobleaching. Arrows indicate stepwise photobleaching. d, Mass photometry spectrum for GAF-ΔPOZ and GAF-FL constructs used in optical tweezer measurements. Spectra show the distribution of protein mass in a sample solution containing the indicated concentration of GAF. Notably, at similar protein concentrations as those used for the optical tweezer experiments (80 nM GAF-FL and 25 nM GAF-ΔPOZ), GAF-FL exists predominantly as an octameric multimer whereas GAF-ΔPOZ exists as a monomer.

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