Genomics Inform.  2008 Mar;6(1):44-49.

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

• Roy DR
• Chandra SB

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 proliferation, differentiation and apoptosis. Comparative analysis of the PKC-alpha, beta, epsilon isozymes of 200 recently sequenced microbial genomes was carried out using variety 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 sequence alignment. S.coelicolor is the subject of our interest because it is notable for the production of pharmaceutically 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 kinase from S. coelicolor can be a good candidate for potent anti-tumor agent. The presence of three representative isotypes of the PKC super family in this organism helps us to understand the mechanism of PKC from evolutionary perspective.

Keyword

eukaryotic type protein; evolution; protein kinase C; Streptomyces coelicolor

MeSH Terms

Anti-Bacterial Agents
Apoptosis
Bacteria
Computational Biology
Genome
Humans
Hydrolysis
Isoenzymes
Negotiating
Phosphotransferases
Protein Kinase C
Protein Kinases
Sequence Alignment
Sequence Analysis
Streptomyces
Streptomyces coelicolor
Threonine
Anti-Bacterial Agents
Isoenzymes
Phosphotransferases
Protein Kinase C
Protein Kinases
Threonine