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

• Published in: Biochimie Vol. 73; no. 10; pp. 1275 - 1280
• Main Authors: Hayes, F., Goumard, G., Hayes, D.H.
• Format: Journal Article
• Language: English
• Published: Paris Elsevier Masson SAS 01.10.1991; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cations, Monovalent; Fundamental and applied biological sciences. Psychology; Holoproteins; Kinetics; Molecular Sequence Data; Other proteins; phosphoamino acid; phosphopeptide; Phosphopeptides - metabolism; phosphoproteins; Phosphorylation; Phosphoserine - metabolism; Phosphothreonine - metabolism; protein; Proteins; ribosomal protein S8; Ribosomal Proteins - chemistry; Ribosomal Proteins - metabolism; ribosome; sodium; Tetrahymena thermophila - metabolism; ribosome; phosphoamino acid; kinetics; phosphopeptide; phosphorylation; protein; Protozoa; Phosphorylation; Tetrahymena thermophila; Aminoacid; Enzymatic digestion; Ciliata; Kinetics; Ribosomal protein; Ion exchange chromatography
• ISSN: 0300-9084; 1638-6183
• DOI: 10.1016/0300-9084(91)90088-I

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 releases a single major phosphoserine containing peptide from both S8′ and S8″, and a single phosphothreonine containing peptide from S8″.