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Monovalent cation‐dependent reversible phosphorylation of a 40 S ribosomal subunit protein in growth‐arrested Tetrahymena : correlation with changes in intracellular pH
Author(s) -
Goumard Geneviève,
Cuny Marguerite,
Sripati Conjeevaram E.,
Hayes Donal H.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80222-5
Subject(s) - dephosphorylation , tetrahymena , phosphorylation , intracellular , protein subunit , intracellular ph , ribosomal protein , chemistry , protein phosphorylation , microbiology and biotechnology , biochemistry , biology , phosphatase , biophysics , ribosome , protein kinase a , rna , gene
Phosphorylation and dephosphorylation of ribosomal protein S8 in starved Tetrahymena induced respectively by Na + and K + are accompanied by changes in intracellular pH which rises by about 0.8 pH units in cells starving in the presence of Na + (phosphorylation of S8) and falls by a little more than one pH unit after subsequent addition of K + (dephosphorylation of S8).