1.Sequence Analysis and Potential Action of Eukaryotic Type Protein Kinase from Streptomyces coelicolor A3(2).
Daisy R ROY ; Sathees B C CHANDRA
Genomics & Informatics 2008;6(1):44-49
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.
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
2.Sequence Analysis and Potential Action of Eukaryotic Type Protein Kinase from Streptomyces coelicolor A3(2).
Daisy R ROY ; Sathees B C CHANDRA
Genomics & Informatics 2008;6(1):44-49
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.
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