Abstract:
The Special AT-rich sequence Binding proteins SATB1 and SATB2 play a significant role in many biological processes ranging from the development of an organism to disease. SATB1 and SATB2 show 61% sequence identity in the amino acid sequence and share the conserved domains. The individual role of these proteins has been studied extensively. However, their role as a complex has not been explored yet. Previously, it has been shown that N-terminal ULD-mediated oligomerization of SATB1 is vital for the high DNA binding affinity and differential regulation of gene expression. Based on these observations, we aimed to identify and characterize the higher-order complex forms of SATB1 and SATB2. Towards that, we found that SATB1 and SATB2 form a complex in cell-based assays. Next, due to failure in the cloning of SATB1, we focused on understanding the oligomeric forms of SATB2. For that, we took biochemical approaches to standardize the expression and purification of SATB2 in the bacterial expression system. Finally, we observed the potential of SATB2 to self-associate using purified proteins by Native Gel Electrophoresis, indicating the higher oligomeric forms of SATB2.
