Localization of adenylate cyclase during development of Dictyostelium discoideum.
Cyclic AMP is known to function as the chemotactic signal during aggregation of single-celled amoebae of the cellular slime mold Dictyostelium discoideum. Evidence from several laboratories has accumulated suggesting that cAMP also acts as a regulatory molecule during Dictyostelium multicellular differentiation. We have used ultramicrotechniques and a sensitive radioimmunoassay in the localization of adenylate cyclase, the cAMP synthetic enzyme, during the development of Dictyostelium. We demonstrate that adenylate cyclase activity is localized in the prespore cells of the culminating individual with no activity detectable in the prestalk region. We show that this lack of activity in the stalk may be due to a masking by an endogenous inhibitor of the enzyme. Within the spore mass we found an increasing gradient of enzyme activity toward the base. These data, along with that from the localization of cyclic nucleotide phosphodiesterase, indicate that an enzymatic potential exists for the creation of cAMP gradients during development in the organism. Such a gradient may provide positional information necessary to direct the terminal differentiation of spore and stalk cells.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D004023:Dictyostelium / Q000201:enzymology / Q000254:growth & development*; D007457:Iodine Radioisotopes; D008832:Microchemistry; D011863:Radioimmunoassay / Q000379:methods; D013172:Spores, Fungal / Q000201:enzymology
D007457:Iodine Radioisotopes; D000262:Adenylyl Cyclases