RNA-binding protein kinase from amphibian oocytes is a casein kinase II

• Published in: FEBS letters Vol. 170; no. 1; pp. 33 - 37
• Main Authors: Kandror, K.V., Stepanov, A.S.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 07.05.1984; Elsevier
• Subjects: Adenosine Triphosphate - metabolism; Amphibia; Amphibian oocyte; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; casein kinase 2; Casein Kinases; Cyclic AMP-independent protein kinase; Electrophoresis, Paper; enzymatic activity; Enzymes and enzyme inhibitors; Female; Freshwater; Fundamental and applied biological sciences. Psychology; Guanosine Triphosphate - metabolism; Heparin - pharmacology; Molecular Weight; oocytes; Oocytes - enzymology; Phosphatase; Protease; Protein Kinases - metabolism; Rana temporaria; RNA - metabolism; RNA-binding protein; serine; sexual cells; threonine; Transferases; tRNA-binding protein; Amphibian oocyte; tRNA-binding protein; Cyclic AMP-independent protein kinase; Phosphatase; Protease; Vertebrata; Phosphoprotein phosphatase; Protein kinase; Substrate specificity; Cyclic AMP; Amphibia; Messenger ribonucleoprotein; Oocyte
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(84)81363-0

RNA-binding protein kinase from amphibian oocytes modifies serine and threonine residues in the molecules of substrates and utilizes both ATP and GTP. Low concentrations of heparin inhibit protein kinase. The foregoing suggests that this enzyme is casein kinase II. It is shown that RNA-binding proteins lack active forms of phosphatases and proteases which may affect the results of phosphorylation of both endogenous and exogenous substrates.