Remote homolog identification of GAGA protein in Mouse (Centre for Cellular & Molecular Biology, Hyderabad, India)

Drosophila transcriptional activator known as GAGA factor, or Trithorax-like, functions by influencing chromatin structure (Granok, 1995). GAGA is a multipurpose protein that mediates gene-specific regulation but also plays a global role in chromosome function. GAGA oligomerization depends on the presence of the N-terminal POZ domain. GAGA was shown to help nucleosome disruption at specific regions of the hsp70 promoter, encompassing GAGA binding sites. At present, little is known about the specific contribution of GAGA to chromatin remodeling, but GAGA appears to be particularly efficient in this respect. Although a direct interaction with the chromatin remodeling machinery cannot be excluded, the simultaneous interaction of GAGA oligomers with multiple adjacent sites could significantly contribute to the higher efficiency of GAGA in disrupting nucleosomes. In this context, it would be interesting to know whether a functional POZ domain is required for efficient nucleosome disruption. I have analyzed the GAGA protein homology and conservation in all the or ganisms through comparative genomics and phylogenetics approach to know about their function and their evolution.