Cyclic AMP-dependent protein kinase from Ustilago maydis
Ustilago maydis was surveyed for cyclic AMP-dependent protein kinase activity. Using a combination of ion-exchange and molecular filtration techniques, we demonstrate that there is only one form of cyclic AMP-dependent protein kinase in the cytosolic fraction of the fungus. The kinase activity is sp...
Guardado en:
Autor principal: | |
---|---|
Otros Autores: | |
Formato: | Capítulo de libro |
Lenguaje: | Inglés |
Publicado: |
Kluwer Academic Publishers
1984
|
Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
Aporte de: | Registro referencial: Solicitar el recurso aquí |
Sumario: | Ustilago maydis was surveyed for cyclic AMP-dependent protein kinase activity. Using a combination of ion-exchange and molecular filtration techniques, we demonstrate that there is only one form of cyclic AMP-dependent protein kinase in the cytosolic fraction of the fungus. The kinase activity is specifically activated by cyclic AMP and utilizes protamine and kemptide as substrates. Most, if not all, of the cyclic AMP binding detected in the soluble fraction is associated with the protein kinase activity. Cyclic AMP-dependent protein kinase is completely dissociated by cyclic AMP into catalytic and regulatory subunits having an apparent molecular weight of 35 000 daltons as judged by sucrose gradient centrifugation. © 1984 Martinus Nijhoff Publishers. |
---|---|
Bibliografía: | Corbin, J., Keely, S., Soderling, T., Park, C., (1975) Adv. Cyclic Nucleot. Res., 5, pp. 265-279 Kelly, P., Cotman, C., (1979) J. Biol. Chem., 254, pp. 1564-1575 Knight, B., Skala, J., (1977) J. Biol. Chem., 252, pp. 5356-5362 Sampson, J., (1977) Cell, 11, pp. 173-180 Fossberg, T., Døskeland, S., Ueland, P., (1978) Arch. Biochem. Biophys., 189, pp. 372-381 Donner, P., Bunte, T., Owada, M., Moelling, K., (1981) J. Biol. Chem., 256, pp. 8786-8794 Moreno, S., Paveto, C., Passeron, S., (1977) Arch. Biochem. Biophys., 180, pp. 225-231 Juliani, M.H., Maia, J.C.C., (1979) Biochim. Biophys. Acta, 567, pp. 347-356 Uno, I., Ishikawa, T., (1974) Biochim. Biophys. Acta, 334, pp. 354-360 Takai, Y., Yamamura, H., Nishizuka, Y., (1974) J. Biol. Chem., 249, pp. 530-535 Powers, P., Pall, M., (1980) Biochem. Biophys. Res. Commun., 95, pp. 701-706 Judewicz, N., Glikin, G., Torres, H.N., (1981) Arch. Biochem. Biophys., 206, pp. 87-92 Corbin, J., Keely, S., Park, C., (1975) J. Biol. Chem., 250, pp. 218-225 Moreno, S., Passeron, S., (1980) Arch. Biochem. Biophys., 199, pp. 321-330 Brochetto-Braga, M., Lopes Gomes, S., Maia, J.C.C., (1982) Arch. Biochem. Biophys., 217, pp. 295-304 Uno, I., Ishikawa, T., (1981) J. Biochem., 89, pp. 1275-1281 Sy, J., Roselle, M., (1981) FEBS Lett., 135, pp. 93-96 Glikin, G., Judewicz, N., Torres, H.N., (1982) Mol. Cell. Biochem., 46, pp. 121-126 Trevillyan, J.M., Pall, M., (1982) J. Biol. Chem., 257, pp. 3978-3986 Gunzberg, J., Veron, M., (1982) Embo J., 1, pp. 1063-1068 Society, (1974) Mycology Guidebook, pp. 507-508. , Mycological Society of America, University of Washington Press, Seattle Gilman, A., (1970) Proc. Natl. Acad. Sci. U.S.A., 67, pp. 305-312 Glynn, I., Chappel, J., (1964) Biochem. J., 90, pp. 147-149 Chang, K., Marcus, N., Cuatrecasas, P., (1974) J. Biol. Chem., 249, pp. 6854-6865 Bradford, M., (1976) Anal. Biochem., 72, pp. 248-254 Lincoln, T., Corbin, J., (1977) Proc. Natl. Acad. Sci. U.S.A., 74, pp. 3239-3244 Leonard, J., Rosenberg, L., (1977) Biochim. Biophys. Acta, 484, pp. 336-348 Beyer, J., (1975) Hoppe-Seyler's Z. Physiol. Chem., 356, pp. 1937-1941 Takai, Y., Yamamura, H., Nishizuka, Y., (1974) J. Biol. Chem., 249, pp. 530-535 Pastori, R., Kerner, N., Moreno, S., Passeron, S., (1981) Biochem. Biophys. Res. Commun., 101, pp. 663-671 |
ISSN: | 03008177 |
DOI: | 10.1007/BF00222481 |