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Characterization of a novel protein inhibitor of protein kinases specific to acidic ribosomal proteins

100%

Pilecki M. , Szyszka R.

tom 39

nr 1

Phosphorylation of acidic ribosomal proteins by ribosome-associated protein kinases of Saccharomyces cerevisiae and Schizosaccharomyces pombe

72%

Jakubowicz T. , Cytrynska M. , Kowalczyk W. , Gasior E.

tom 40

nr 4

Two proteins of 13 kDa and 38 kDa, the components of 60S ribosomal subunits, were identified as phosphorylation substrates for protein kinases tightly associated with S. cerevisiae and Schizosaccharomyces pombe ribosomes. An enzyme with properties of multifunctional casein kinase II was detected in ribosome preparations from both yeast species. In S. cerevisiae another protein kinase with high substrate specificity toward those proteins was also identified. By using isoelectric focusing, the protein band of 13 kDa from S. cerevisiae and S. pombe was resolved respectively into three and four major forms of different charge. The same protein forms were phospho- rylated in the in vivo 32P-labelling experiments.