Phosphorylation of Ribosome-Associated Protein by an Adenosine 3′:5′-Cyclic Monophosphate-Dependent Protein Kinase: Location of the Microsomal Receptor and Protein Kinase
Author(s) -
Gordon M. Walton,
Gordon N. Gill,
Itamar B. Abrass,
Leonard D. Garren
Publication year - 1971
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.5.880
Subject(s) - protein kinase a , ribosome , biochemistry , protein kinase r , endoplasmic reticulum , cgmp dependent protein kinase , eukaryotic ribosome , mitogen activated protein kinase kinase , chemistry , biology , phosphorylation , rna , gene
In the adrenal cortex, the adenosine 3′:5′-cyclic monophosphate (cAMP)-receptor protein and the cAMP-dependent protein kinase are located in both the cytosol and endoplasmic reticulum. The cAMP-dependent protein kinase from the cytosol catalyzes the phosphorylation of ribosome-associated protein. Ribosomes washed in 0.5 M NH4 Cl retain the substrate of the protein kinase reaction, but are dependent on the NH4 Cl extract forin vitro protein synthesis. Dissociation of the 80S ribosomes by 0.88 M KCl, however, releases the ribosome-associated (protein) substrate of the phosphorylation reaction.
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