Abstract
Phosphorylation of ribosomal acidic proteins ofSaccharomyces cerevisiae is an important mechanism regulating a number of active ribosomes. The key role in the regulatory mechanism is played by specific phosphoprotein kinases and phosphoprotein phosphatases. Three different cAMP-independent protein kinases phosphorylating acidic ribosomal proteins have been identified and characterized. The protein kinase 60S (PK60S), RAP kinase, and casein kinase type 2 (CK2). All three protein kinases phosphorylate serine residues which are localized in the C-terminal end of phosphoproteins. Synthetic peptides were used to determinate the amino acid sequence of phosphoacceptor site for PK60S. Peptide AAEESDDD derived from phosphoproteins YP1β/β′ and YP2α turned out to be the best substrate for PK60S. A number of halogenated benzimidazoles and 2-azabenzimidazoles were tested as inhibitors of the three protein kinases. 4,5,6,7-Tetrabromo-2-azabenzimidazole inhibits phosphorylation only of these polypeptides phosphorylated by protein kinase 60S, namely YP1β/β′ and YP2α, but not the other, YP1α and YP2β phosphorylated by protein kinases RAP and CK2. RAP kinase has been found in an active form in the soluble fraction ofS. cerevisiae. The enzyme uses ATP as a phosphate donor and is less sensitive to heparin than casein kinase 2. RAP kinase monophosphorylates the four acidic proteins. The ribosome-bound proteins are a better substrate for the enzyme. Multifunctional CK2 kinase phosphorylate all four acidic proteins. The kinase phosphorylates preferentially serine or threonine residues surrounded by cluster of acidic residues. The enzyme activity is stimulatedin vitro by the presence of polylysine and inhibited by heparin.
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Abbreviations
- CK2:
-
protein kinase CK2 (hitherto known as casein kinase type 2 and/or casein kinase II)
- PK60S:
-
protein kinase 60S ribosomal subunits
- RAP kinase:
-
ribosomal acidic protein kinase
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Szyszka, R. Protein kinases phosphorylating acidic ribosomal proteins from yeast cells. Folia Microbiol 44, 142–152 (1999). https://doi.org/10.1007/BF02816233
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DOI: https://doi.org/10.1007/BF02816233