Sequence Analysis and Potential Action of Eukaryotic Type Protein Kinase from Streptomyces coelicolor A3(2)

Abstract

Abstract Protein kinase C (PKC) is a family of kinases involved in the transduction of cellular signals that promote lipid hydrolysis. PKC plays a pivotal role in mediating cellular responses to extracellular stimuli involved in prolifer-ation, differentiation and apoptosis. Comparative analy-sis of the PKC-α,β,e isozymes of 200 recently se-quenced microbial genomes was carried out using varie-ty of bioinformatics tools. Diversity and evolution of PKC was determined by sequence alignment. The ser/thr protein kinases of Streptomyces coelicolor A3 (2), is the only bacteria to show sequence alignment score greater than 30% with all the three PKC isotypes in the se-quence alignment. S.coelicolor is the subject of our in-terest because it is notable for the production of phar-maceutically useful compounds including anti-tumor agents, immunosupressants and over two-thirds of all natural antibiotics currently available. The comparative analysis of three human isotypes of PKC and Serine/ threonine protein kinase of S.coelicolor was carried out and possible mechanism of action of PKC was derived. Our analysis indicates that Serine/ threonine protein kin-ase from S. coelicolor can be a good candidate for po-tent anti-tumor agent. The presence of three representa-tive isotypes of the PKC super family in this organism helps us to understand the mechanism of PKC from evolutionary perspective. Keywords: eukaryotic type protein, evolution, protein kinase C, Streptomyces coelicolor