Monovalent cation-dependent reversible phosphorylation of ribosomal protein S8 in growth arrested Tetrahymena: kinetics of formation, phosphoamino acids, and phosphopeptides of mono-, and diphosphorylated derivatives of protein S8.
The kinetics of formation of mono-, and diphosphorylated derivatives of ribosomal protein S8 in Tetrahymena starving in the presence of Na+ have been determined, and the phosphoamino acids present in these derivatives have been identified. The mono-phosphorylated product, S8', contains only phosphoserine, and behaves kinetically as the precursor of the diphosphorylated product S8" which contains phosphoserine, and phosphothreonine. Tryptic digestion release a single major phosphoserine containing peptide from both S8' and S8", and a single phosphothreonine containing peptide from S8".
Hayes
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Laboratoire de Chimie Cellulaire, Institut de Biologie Physico-Chimique, Paris, France.
Goumard
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Hayes
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D000595:Amino Acid Sequence; D000818:Animals; D002414:Cations, Monovalent; D007700:Kinetics; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism*; D016808:Tetrahymena thermophila / Q000378:metabolism*
D002414:Cations, Monovalent; D010748:Phosphopeptides; D012269:Ribosomal Proteins; C030254:ribosomal protein S8; D010769:Phosphothreonine; D010768:Phosphoserine