Genomics & Informatics

  • 제6권1호
  • /
  • Pages.44-49
  • /
  • 2008
  • /
  • 1598-866X(pISSN)
  • /
  • 2234-0742(eISSN)
한국유전체학회 (Korea Genome Organization)
권호 표지
DOI QR코드

DOI QR Code

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

  • Roy, Daisy R. (Department of Biological, Chemical and Physical Sciences, Roosevelt University) ;
  • Chandra, Sathees B.C. (Department of Biological, Chemical and Physical Sciences, Roosevelt University)
  • 발행 : 2008.03.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

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-${\alpha},{\beta},{\varepsilon}$ 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.

키워드

참고문헌

  1. Bentley, S.D., Charter, K.F., Cerdeno Tarraga, A.M., Challis, G.L., Thomson, N.R., James, K.D., Harris, D.E., Quail, M.A., Kieser, H., Harper, D., Batemen, A., Brown, S., Chandra, G., Chen, C.W., Collins, M., Cronin, A., Fraser, A., Globle, A., Hidalgo, J., Hornsby, T., Howartg, S., Huang, C.H., Kieser, T., Larke, L., Murphy, L., Oliver, K., O'Neil, S., Rabbinowitsch, E., Rajandream, M.A., Rutherford, K., Rutter, S., Seeger, K., Saunders, D., Sharp, S., Squares, S., Taylor, K., Warren, T., Wietzorrek, A., Woodward, J., Barrell, B. G., Parkhill, J., and Hopwood, D.A. (2002). Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417, 141-147. https://doi.org/10.1038/417141a
  2. Chen, K.H., Peng, Z.G., Lavu, S., and Kung, H.F. (1989). Molecular cloning and sequence analysis of two distinct types of Xenopus laevis protein kinase C. Second messengers Phosphoproteins 12, 251-260.
  3. Filner, P. (1999). Protein kinase C: possibly a drug target for inhibiting neovascularization in wet age-related macular degeneration. MD Foundation Inc, Macular Degeneration Research Fund. October 31
  4. House, C., and Kemp, B.E. (1987). Protein kinase C contains a pseudosubstrate prototype in its regulatory domain. Science 238, 1726-1728. https://doi.org/10.1126/science.3686012
  5. Jimenez, B., Pestana, A., and Fernandez-Renart, M. (1989). A phospholipid-stimulated protein kinase from Dictyostelium discoideum. Biochem. J. 260, 557-561. https://doi.org/10.1042/bj2600557
  6. Luderus, M.E.E., Van der Most, R.G., Otte, A.P., and Driel, R.V. (1989). A protein kinase C related enzyme activity in Dictyostelium discoideum. FEBS Lett. 253, 71-75. https://doi.org/10.1016/0014-5793(89)80932-9
  7. Mellor, H. and Parker, J.P. (1998). Review: the extended protein kinase C super family. Biochem. J. 332, 281-292. https://doi.org/10.1042/bj3320281
  8. Newton, A.C. (1995). Protein kinase C: structure, function and regulation. J. Biol. Chem. 270, 48, 28495-28498. https://doi.org/10.1074/jbc.270.48.28495
  9. Nishizuka, Y. (1995). Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9(7), 484-496. https://doi.org/10.1096/fasebj.9.7.7737456
  10. Ogita, K., Miyamoto, S., Koide, H., Iwai, T., Oka, M., Ando, K., Kishimoto, A., Ikeda, K., Fukami, Y., and Nishizuka, Y. (1990). Protein kinase C in Saccharomyces cerevisiae: comparison with the mammalian enzyme. PNAS . 87, 5011-5015. https://doi.org/10.1073/pnas.87.13.5011
  11. Orr, J.W., and Newton, A.C. (1994). Intrapeptide regulation of protein kinase C. J. Biol. Chem. 269(11), 8383-8387.
  12. Schaeffer, E., Smith, D., Mardon, G., Quinn, W., and Zuker, C. (1989). Isolation and characterization of two new drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells. Cell 57, 403-412. https://doi.org/10.1016/0092-8674(89)90915-X
  13. Shen, S.S., and Ricke, L.A. (1989). Protein Kinase C from sea urchin eggs. Comp Biochem. Physiol . B. 92, 251-254. https://doi.org/10.1016/0305-0491(89)90274-5
  14. Winstead, E.R. (2002). Medicinal microbe Streptomyces coelicolor is sequenced. Genome News Network . May 9
  15. Yoshiji, H., Kuriyama, S., Ways, D.K., Yoshii, J., Miyamoto, Y., Kawata, M., Ikenaka, Y., Tsujinoue, H., Nakatani, T., Shibuya, M., and Fukui, H. (1999). Protein kinase C lies on the signaling pathway for vascular endothelial growth factor-mediated tumor development and angiogenesis. Cancer Res. 59, 4413-4418.