Elucidation of dynamics and function of an iPS cell reprogramming factor Sox2 from the view point of an intrinsically disordered protein

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NMR relaxation dispersion studies revealed that Sox2 fluctuates when it is free in solution, in particular the N-terminal helix α1 and the regions contacting the helixα1 are unfolded with a population of 2%. In contrast, no relaxation dispersion was observed for Sox2 in the bound form, indicating that Sox is stable in the bound form on μs-ms timescales. Since the helix α1 binds directly to DNA, the fluctuation observed for the free form is supposed to be important for non-specific binding to DNA.