Abstract
Even under physiological condition, a variety of base damages are created and these are mainly repaired by base excision repair (BER) pathway. Considering the paucity of damaged bases within the genome, the cell should have a very efficient system for searching them. Human N-methylpurine DNA glycosylase (hMPG) is a BER protein which initiates repair of a diverse group of alkylated and deaminated purines, and can diffuse along the DNA to find base lesions. And many proteins such as nucleotide excision repair (NER) related protein or transcriptional control elements interact with hMPG to regulate the activity. However, the exact damage detection mechanism of hMPG is not fully understood. In the present study, we have focused to identifying proteins interact with hMPG. We cloned an Escherichia coli strain expressing GST-fused hMPG. Now we are investigating HeLa cell nuclear proteins which interact with GST-hMPG using pulldown assay and mass spectrometry.
