Endogenous substrates for protein kinases in Coprinus macrorhizus.
The phosphorylation of cellular proteins in mycelia in strain Fisc in Coprinus macrorhizus was examined. The phosphorylation of two proteins, Protein A and B, was stimulated by cyclic AMP in the presence of Mg2+, and that of one protein, Protein C, was inhibited by cyclic AMP. The molecular weight of these proteins was determined, by gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), to be 64000 (Protein A), 46000 (Protein B), and 18000 (Protein C), respectively. These proteins were quickly phosphorylated and the phosphorylation reached to the maximal levels in 5 min. The concentration of cyclic AMP required for the half-maximal stimulation of phosphorylation of Protein A and B, and for the half-maximal inhibition of phosphorylation of Protein C was approx. 1.0 x 10(-7) M. Cyclic GMP and cyclic IMP were slightly effective for stimulation and inhibition of these proteins.
D000363:Agaricales / Q000201:enzymology*; D003302:Coprinus / Q000201:enzymology*; D000242:Cyclic AMP / Q000494:pharmacology; D005656:Fungal Proteins / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D005656:Fungal Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D008274:Magnesium