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Phosphorylation of ribosomal proteins by ribosome‐associated protein kinases of Trichosporon cutaneum
Author(s) -
Wojda Iwona,
Cytryńska Malgorzata,
Jakubowicz Teresa
Publication year - 1996
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620360511
Subject(s) - ribosomal protein , ribosome , phosphoprotein , biochemistry , phosphorylation , biology , casein kinase 1 , casein kinase 2 , kinase , protein phosphorylation , eukaryotic ribosome , protein kinase a , protein subunit , microbiology and biotechnology , mitogen activated protein kinase kinase , rna , gene
Four ribosomal proteins of Mr 13 kDa, 15 kDa, 19 kDa and 38 kDa were identified as phosphorylation substrates for protein kinases tightly associated with Trichosporon cutaneum ribosomes. It was found that proteins of 13 kDa, 19 kDa and 38 kDa were phosphorylated by multifunctional casein kinase II while the protein of 15 kDa by casein kinase I. Proteins of 13 kDa and 38 kDa were detected in the large subunits while 15 kDa and 19 kDa in the small ribosomal subunits. By using isoelectrofocusing the protein of 13 kDa was resolved into two individual phosphorylated forms. The phosphorylation level of both forms was much higher in ribosomes from the cells collected at the exponential growth phase than in those from the stationary phase. The same phosphoprotein forms were identified in ribosomes from in vitro and in vivo [ 32 P]‐labelling experiments.