An increase of cAMP-dependent protein kinase during development in Polysphondylium pallidum.
Polysphondylium pallidum is a cellular slime mold in which, unlike in Dictyostelium discoideum, cAMP is not the chemotactic agent. The occurrence of a cAMP-dependent protein kinase in D. discoideum was demonstrated earlier and we suggested that it may mediate the intracellular effects of cAMP on the development of the organism, particularly since an increase in the amount of the enzyme during development was noted. In D. discoideum cAMP plays a dual role insofar as it serves both as chemotactic agent and as second messenger; it was of interest therefore, to determine whether a cAMP-dependent protein kinase occurred in P. pallidum. We found a cAMP-dependent protein kinase in P. pallidum using Kemptide as substrate. The regulatory subunit of the enzyme has an apparent molecular weight of 41,000 and seems to be similar in its properties with that isolated earlier from D. discoideum. The cAMP-dependent protein kinase catalytic subunits from the two species are also similar. Furthermore, there is a developmentally regulated, parallel, two- to threefold increase in the two subunits of the cAMP-dependent protein kinase in P. pallidum. The increase occurs before aggregates are formed. These findings are compatible with a role of the intracellular cAMP and of the cAMP-dependent protein kinase in the development of P. pallidum.
D003624:Darkness; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009235:Myxomycetes / Q000201:enzymology* / Q000254:growth & development; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*
D046911:Macromolecular Substances; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases