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• W2092806446 startingPage "395" @default.
• W2092806446 abstract "Phosphorylation of ribosomal proteins in vivo was studied in exponentially growing and starved cells of the ciliated protozoan, Tetrahymena pyriformis. No phosphorylation of ribosomal proteins could be demonstrated in cells growing exponentially in complex nutrient media. However, when Tetrahymena cells were transferred into a non-nutrient medium, pronounced phosphorylation of a single ribosomal protein was observed. During two-dimensional polyacrylamide gel electrophoresis the phosphorylated ribosomal protein migrated in a manner virtually identical to that of the phosphorylated ribosomal protein S6 of rat liver. The phosphorylated ribosomal protein has a molecular weight of 38 000 as estimated by dodecylsulfate polyacrylamide gel electrophoresis. Thus, the phosphorylated ribosomal protein found in starved Tetrahymena is apparently homologous with the ribosomal protein which is predominantly phosphorylated in higher eukaryotes. When phosphorylated ribosomes were dissociated by treatment with high concentration of KCl, the phosphorylated protein was found only on the small subunit. If dissociation was achieved by dialysis against a buffer low in MgCl2, the phosphorylated protein was distributed almost equally between the two subunits. This indicates that the phosphorylated ribosomal protein is located at the interface between the two subunits." @default.
• W2092806446 created "2016-06-24" @default.
• W2092806446 creator A5000185465 @default.
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• W2092806446 creator A5017132939 @default.
• W2092806446 date "1978-02-01" @default.
• W2092806446 modified "2023-09-25" @default.
• W2092806446 title "Phosphorylation in vivo of Ribosomes in Tetrahymena pyriformis" @default.
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• W2092806446 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12105.x" @default.
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