Elucidating a DNA recognition mechanism of a transcriptional factor protein by characterizing dynamic processes of specific/non-specific DNA-bound complexes

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Transcriptional factor sox2 is a one of the major factor gene used for induced pluripotent stem cell (iPSC) technologies. Sox2 possesses a high-mobility group box (HMG) domain, which specifically binds to only 6-7 bp of DNA to exert its function. However, DNA recognition mechanism of sox2 is not fully understood. In this study, to elucidate how sox2 recognizes the target sequence, we investigated dynamics of the HMG domain upon DNA binding using NMR. We found that the HMG domain is flexible and almost unfolded in the absence of DNA. However, when the HMG domain binds to the target sequences, the HMG domain forms stable structure with DNA. This study revealed that the unfolded structure of the HMG domain is stabilized upon DNA binding.