Biokhimiia 1983 Oct 01;4810:1674-9.

[Protein kinase, phosphatase and protease activities in a fraction of RNA-binding proteins].

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The RNA-binding proteins from amphibian (Rana temporaria and Xenopus laevis) oocytes contain a cAMP-independent caseintype protein kinase activity. This enzyme can phosphorylate casein but does not phosphorylate histones. Using high voltage paper electrophoresis of acid hydrolysate of [32P]casein, it was found that P-O-phosphoserine and [32P]-O-phosphothreonine are formed via the phosphorylation reaction. Protein kinase retains the ability to bind poly(U) under physiological ionic strength values. It was shown that RNA-binding proteins do not contain any detectable forms of phosphatase or protease which might distort the results of phosphorylation of endogenous and exogenous substrates.

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Genes referenced: camp