Comparative analysis of protein phosphatases in Arabidopsis genome

초록

Reversible phosphorylation is a critically important step in the functional regulation of a protein. Protein kinases and protein phosphatases which respectively add and remove phosphate group of target proteins, constitute about 2-4% of the genes in a typical eukaryotic genome. Recently, protein phosphatases are evolving as important players in many cellular processes such as proliferation, differentiation, cell adhesion and motility. Now protein phosphatases are amongst the extensively studied proteins and are reported as potential drug targets of many diseases including cancer and others. Here, we identified at least 142 putative protein phosphatases in Arabidopsis genome. We classified these proteins into five groups on the basis of the catalytic protein phosphatase domains present on them. We analyzed the expression profiles of each Arabidopsis phosphatases. We modeled three dimensional structures of these proteins. We performed in silico docking of Arabidopsis PP2A with okadaic acid and calculated the affinity energy (-10.9kcal/mol) between them. Furthermore, we extended our study in rice genome to find out the Arabidopsis protein phosphatase orthologs in rice.