Sequence Analysis and Potential Action of Eukaryotic Type Protein Kinase from Streptomyces coelicolor A3(2)
Genomics & Informatics
;
: 44-49, 2008.
Article
in English
| WPRIM
| ID: wpr-142399
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phosphotransferases
/
Protein Kinases
/
Streptomyces
/
Threonine
/
Bacteria
/
Protein Kinase C
/
Sequence Alignment
/
Negotiating
/
Genome
/
Sequence Analysis
Limits:
Humans
Language:
English
Journal:
Genomics & Informatics
Year:
2008
Type:
Article
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