Adenosine 3',5'-monophosphate-receptor protein and protein kinase in Coprinus macrorhizus.
A single cAMP-receptor protein could be detected in mycelial extracts of Coprinun macrorhizus by using the photoaffinity cAMP-analogue, 8-N3-cAMP. The protein which specifically bound 32P-labeled 8-N3-cAMP had an apparent molecular weight of 46,000 as determined by an SDS-polyacrylamide gel electrophoresis system. The 46,000-dalton protein was characterized by the dissociation constant for [32P]-8-N3-cAMP, and by the nucleotide specific inhibition of [32P]-8-N3-cAMP binding. The 46,000-dalton protein was co-chromatographed on a DEAE-cellulose column with cAMP-dependent protein kinase. The levels of [32P]-8-N3-cAMP-binding and protein kinase activities in mycelial extracts of strains used was always in parallel. The result indicated that the 46,000-dalton protein may be a regulatory subunit of protein kinase with the capacity to bind cAMP. cAMP-dependent protein kinase of this fungus was immunologically different from those of higher animals.
D001386:Azides; D001487:Basidiomycota / Q000032:analysis*; D002352:Carrier Proteins / Q000032:analysis*; D002848:Chromatography, DEAE-Cellulose; D000242:Cyclic AMP / Q000031:analogs & derivatives / Q000032:analysis* / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein; D008970:Molecular Weight; D009712:Nucleotides, Cyclic / Q000378:metabolism; D011494:Protein Kinases / Q000032:analysis*
D001386:Azides; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D009712:Nucleotides, Cyclic; C017042:8-azidoadenosine-3',5'-monophosphate; D000242:Cyclic AMP; D011494:Protein Kinases