Expression and purification of recombinant active ten-eleven translocation enzyme in escherichia coli

Increasing research on epigenetics in recent years and the inability to explain some of the subjects with genetically, have necessitated the uncovering of epigenetic mechanisms. As a result of the epigenetic studies made, it has been found that the deterioration of the epigenetic mechanisms is associated with many neurodegenerative diseases and especially cancer. DNA methylation is one of the most common epigenetic mechanisms. In recent years, studies have revealed the existence of a protein family called TET (ten-eleven translocation), which is responsible for DNA demethylation. These proteins have been shown to actively reverse DNA methylation and to significantly affect the epigenetic control mechanism through the methylcytosine derivatives they form. However, the mechanism of the TET proteins on the highly complex epigenetic changes is still unclear. The kinetic behavior of proteins is thought to be one of these mechanisms of action. One of the most important thing needed at this point is the production of active TET proteins in a large amount in order to study kinetic and mechanistic of TET proteins. In this study, it was aimed to purify the catalytic domain of TET1 protein recombinantly and actively in E. Coli bacteria.