Investigating the putative phosphorylation of PfHDAC1 by PfCKII and its possible role in gene regulation

Abstract

Even though artemisinin based combination therapies have made remarkable progress in reducing the number of malaria infections globally, the acquisition of resistance against these drugs by the parasite Plasmodium falciparum is also getting reported with time. Histone deacetylase 1 (HDAC 1) belonging to Class I HDACs is a potential regulator of artemisinin resistance phenotype and phosphorylation status of HDAC1 plays an important role in controlling its activity. Casein Kinase II (CKII) is a regulator of phosphorylation of Class I HDACs in higher eukaryotes. In Plasmodium, CKII is present in the interactome of artemisinin. In this study, we show that PfHDAC1 gets phosphorylated by PfCKII through in-vitro assays. We also demonstrate that deacetylase activity of PfHDAC1 is enhanced by PfCKII phosphorylation.