PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
1999 | 46 | 4 |

Tytuł artykułu

SDS-PAGE characteristics of protein kinases tightly associated with chick embryo brain ribosomes

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Protein kinases tightly associated with chick embryo brain ribosomes washed with Triton X-100 and KCl were characterized by their ability to phosphorylate ribosomes and two exogenous substrates, histone IIA and casein. c-AMP-dependent kinase (PKA) and casein kinases (CK1, CK2) were examined in the presence of specific modulators by SDS/ PAGE followed by renaturation in gel assay according to Kameshita & Fujisawa (Anal. Biochem. 1989, 183, 139-143). Basing on these data it can be presumed that PKA activity increases, but the levels of CK2 and CK1 decrease during chick embryo development.

Wydawca

-

Rocznik

Tom

46

Numer

4

Opis fizyczny

p.911-917,fig.

Twórcy

  • Medical Academy, 20-123 Lublin, Lubartowska 85, Poland

Bibliografia

  • 1. De-Haro, C., Mendez, R. & Santoyo, J. (1996) The eIF-2 alfa kinases and the control of pro­tein synthesis. FASEBJ. 10, 1378-1387.
  • 2. Zhu, S. & Wek, R.C. (1998) Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control. J. Biol Chem. 27». 1808-1814.
  • 3. Traugh, J.J. (1989) Approaches to examine the role of multiple serine protein kinase in the coordinate regulation of growth; in Ad­vances in Regulation of Cell Growth (Monod, J.J., Cambier, J.C. & Weiss, A., ed.) vol. 1, pp. 173-201, Academic Press, New York.
  • 4. Ballesta, J.P.G. & Remacha, M. (1996) The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational ma­chinery. Prog. Nucleic Acid Res. Mol Biol 55, 157-193.
  • 5. Vard, C., Guillot, D., Bargis, P., Lavergne, J.P. & Reboud, J.P. (1997) A specific role for the phosphorylation of mammalian acidic ribo­somal protein P2. J. Biol Chan. 272, 20259-20262.
  • 6. Sanecka-Obacz, M. (1984) Phosphorylation of brain and liver ribosomal proteins during early development of chick embryo. Acta Physiol Pol 35, 346-354.
  • 7. Sanecka-Obacz, M. (1988) Developmental changes in the protein kinase activity of chick brain. Acta Physiol Pol 39, 143-150.
  • 8. Sanecka-Obacz, M. & Jakubowicz, T. (1998) Comparative analysis of phosphorylation by ribo8ome bound protein kinases from Saccharomyces cereuisiae and chick embryo brain. Bull Pol Ac.: Biol 46, 1-6.
  • 9. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
  • 10. Kameshita, I. & Fujisawa, H. (1989) A sensi­tive method for detection of calmodulin-de- pendent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal Biochem. 183, 139-143.
  • 11. Sanchez-Madrid, F., Vidales, F., Ballesta, J.P.G. (1981) Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosome. Eur. J. Biochem. 114, 609-613.
  • 12. Cytryńska, M., Wojda, I. & Jakubowicz, T. (1995) The acidic ribosomal proteins of differ­ent yeast species. Phosphorylation by ribo­some associated protein kinases. J. Microbiol 35, 367-373.
  • 13. Pilecki, M., Grankowski, N., Jacobs, J. & Gąsior, E. (1992) Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins. Eur. J. Biochem. 206, 259-267.
  • 14. Cochet, C. & Chambaz, E.M. (1983) Poly- amine-mediated protein phosphorylations: A possible target for intracellular polyamine ac­tion. Mol Cell Endocrinol. 30, 247-266.
  • 15. Hathaway, G.M. & Traugh, J.A. (1982) Casein kinases-multipotential protein kinases. Curr. Top. Cell Regul. 21, 101-127.
  • 16. Zhai, L., Graves, P.R., Robinson, L.C., Italiano, M., Culbertson, M.R., Rowles, J., Cobb, M.H., DePaoli-Roach, A.A. & Roach, P J. (1995) Casein kinase Iy subfamily. Molec­ular cloning, expression, and characterization of three mammalian iaoforms and comple­mentation of defects in the Saccharomyces cerevisiae YCK genes. J. Biol Chem. 270, 12717-12724.
  • 17. Qi, Z., Zhu, X., Goedert, M., Fujita, D.J. & Wang, J.H. (1998) Effect of heparin on phosphorylation site specificity of neuronal Cdc2-like kinase. FEBS Lett. 423, 227-230.
  • 18. Pinna, L.A. & Meggio, F. (1997) Protein kinase CK2 ("casein kinase-2") and its implica­tion in cell division and proliferation; in Prog­ress in Cell Cycle Research (Meijer, L., Guidet, S. & Philipe. M., eds.) vol. 3, pp. 77-97, Ple­num Press, New York.
  • 19. Lin, W.-J., Tuazon, P.T. & Traugh, J.A. (1991) Characterization of the catalytic subunit of ca­sein kinase II expressed in Escherichia coli and regulation of activity. J. Biol Chem. 266, 5664-5669.
  • 20. Valero, E., De Bonis, S., Filhol, 0., Wade, R.H., Langowski, J., Chambaz, E.M. & Cochet, C. (1995) Quarternary structure of casein kinase 2. Characterization of multiple oligo- meric states and relation with its catalytic ac­tivity. J. Biol Chem. 270, 8345-8352.
  • 21. Bregman, D.B., Bhattacharya, N. & Rubin, C.S. (1989) High affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II-B. Cloning, characterization, and expression of cDNAs for rat brain pl50. J. Biol Chem. 264, 4648-4656.
  • 22. Li, Y. & Rubin, C.S. (1995) Mutagenesis of the regulatory subunit (RUß) of the cAMP-depend- ent protein kinase II ß reveals hydrophobic amino acids that are essential for RII/9 dimerization and/or anchoring RUß to the cytoskeleton.J. Biol Chem. 270,1935-1944.
  • 23. Kim, J.M., Cha, D.R. & Bae, Y.S. (1996) Inter­action of the beta subunit of casein kinase II with the ribosomal protein L5. Biochem. Biophys. Res. Commun. 226, 180-186.
  • 24. Lee, J.H., Kim, J.M., Lee, Y.T., Marshak, D.R. & Bae, Y.S. (1997) The highly basic ribosomal protein L41 interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of topoisomerase II alpha by CKII. Biochem. Biophys. Res. Commun. 238, 462-467.
  • 25. Plana, M., Gil, C., Molina, E. & Itarte, E. (1994) Protein kinase CKII: Possible regula­tion by interaction with protein substrates. Cell Mol Biol Res. 40, 455-461.
  • 26. Gil. C., Plana, M., Riera, M. & Itarte, E. (1996) Rat liver pp49, a protein that forms complexes with protein kinase CK2, is composed of the/? and the y subunits of translation initiation fac­tor eIF-2. Biochem. Biophys. Res. Commun. 225, 1052-1057.
  • 27. Wang, P.C., Vancura, A., Mitcheson, T.G. & Kuret, J. (1992) Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1. Mol Biol Cell 3, 275-286.
  • 28. Brockman, J.L., Gross, S.D., Sussman, M.R. & Anderson, R.A. (1992) Cell cycle-dependent lo­calization of casein kinase I to mitotic spin­dles. Proc. Natl Acad. ScL U.S.A. 89, 9454- 9458.
  • 29. Kuret, J., Johnson, G.S., Cha, D., Christenson, E.R., DeMaggio, A.J. & Hoekstra, M.F. (1997) Casein kinase I is tightly associated with paired-helical filaments isolated from Alzhei­mer's disease brain. J. Neurochem. 69, 2506-2515.
  • 30. Longenecker, K.L., Roach, P.J. & Hurley, T.D. (1996) Three dimensional structure of mam­malian casein kinase I: Molecular basis for phosphate recognition. J. Mol Biol. 257, 618-631.
  • 31. Mclnnes, C. & Leader, D.P. (1997) Tis- sue-specific distribution of mouse casein kinase I alfa mRNA. DNASeq. 8, 55-57.
  • 32. Zhang, J., Gross, S.D., Schroeder, M.D. & An­derson, R.A. (1996) Casein kinase I alfa and alfa L: Alternative splicing-generated kinases exhibit different catalytic properties. Biochem­istry 35, 16319-16327.
  • 33. Haas, D.W. & Traugh, J.A. (1991) Casein kinase I phosphorylates the 25-kDa mRNA cap-binding protein. Arch. Biochem. Biophys. 284, 84-89.
  • 34. Desdouits, F., Cohen, D.f Nairn, A.C. & Greengard, P. (1995) Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo. J. Biol Chem. 270, 8772-8778.
  • 35. Dubois, T., Rommel, C., Howell, S., Stei- hussen, U., Soneji, Y., Morrice, N., Moelling, K. & Aitken, A. (1997) 14-3-3 is phospho- rylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J. Biol Chem. 272, 28882-28888.
  • 36. Nestler, E.J. & Greengard, P. (1984) Protein phosphorylation as a conceptual frame work for investigation of biological regulation; in Protein Phosphorylation in the Nervous System, pp. 1-16, Neuroscience Institute Publication, Wiley, New York.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-4cc24e05-e52a-4fb8-ab3a-dd997af4bb5f
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.