Figure 1.

Biochemical function of GFI1 as a transcription factors. Schematic depiction of GFI1 in a complex with its interacting proteins occupying a genomic site 5′ of a target gene. Whereas, the recruitment of the LSD1/CoRest complex occurs through the N-terminal SNAG domain (green), the middle domain (gray) serves mainly as an interaction platform for other proteins and the C₂H₂ zinc finger domains (blue) mediate DNA binding. G9A and HDACs can bind directly to GFI1, but HDACs can also be part of the LSD1/CoRest complex. HDACs and LSD recruitment leads to the removal of acetyl- or methyl groups from Histone H3 lysine 9 or 4, respectively. G9A enables the methylation of H3 lysine 9.