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  • Title: [Inhibition of casein kinase type 2 activity by formation of complexes with mRNA in vivo].
    Author: Kandror KV, Stepanov AS.
    Journal: Biokhimiia; 1990 Sep; 55(9):1584-9. PubMed ID: 2127728.
    Abstract:
    It is known that casein kinase 2 possesses, besides the protein kinase, an RNA-binding activity. Using ligand blotting it has been demonstrated that the both activities are localized on the alpha- and alpha'-subunits of the enzyme. Casein kinase 2 is suppressed in vitro by polyuridylic acid. A part of the intracellular pool of casein kinase 2 is found in the informosomes. The informosomes and free proteins were separated by centrifugation in a sucrose density gradient, and each fraction was incubated with casein and [gamma-32P]ATP. The informosome-bound protein kinase is completely inhibited, while the free protein kinases heavily phosphorylate casein. It is concluded that the activity of casein kinase 2 can be regulated by the reversible formation of complexes with RNA.
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