Circular Dichroism Studies on C-terminal Zinc Finger Domain of Transcription Factor GATA-2

The C-terminal zinc finger domain of GATA-2 transcription factor from Rattus norvegicus has been expressed and purified to elucidate its secondary structure using circular dichroism spectroscopy. Circular dichroism spectra showed that native GATA-2 C-terminal domain of (Cys)4 type zinc finger has 12% α-helix, 36% β-sheet and 52% random coil content. The estimated structure was compared with predicted structures by sequence based prediction software SOPMA and found to be similar. Furthermore, the effect of pH on the secondary structure of GATA-2 C-finger was examined. This study provides an insight into the understanding of the structure and function of transcription factor GATA-2.