Synthetic phosphopeptides are substrates for casein kinase II

FEBS Letters

Arendt, Anatol²  Palczewski, Krzysztof²  Hargrave, Paul A.²  Lozeman, Fred J.¹  W. Litchfield, David¹  Krebs, Edwin G.¹ 

[1] Howard Hughes Medical Institute and the Department of Pharmacology, Mail Stop SL-15, University of Washington, Seattle, WA 98195 USA;Department of Ophthalmology and Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA

关键词: Casein kinase 2;    Substrate specificity;    Synthetic phosphopeptide;    Peptide phosphorylation;    TFA;    trifluoroacetic acid;    boc;    t-butoxycarbonyl;    HOBt;    1-hydroxybenzotriazole;    DIG;    1;    3-diisopropylcarbodiimide;   

DOI  :  10.1016/0014-5793(90)80650-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Casein kinase II is a protein serine/threonine kinase that exhibits a preference for acidic substrates. Previous studies have demonstrated that a glutamic acid 3 amino acids C-terminal (+3) to a serine or threonine is required for phosphorylation. To examine the ability of phosphoserine and phosphothreonine residues to serve as specificity determinants for casein kinase II, phosphopeptides containing either of these phosphoamino acids in the +3 position were synthesized and tested as substrates. Phosphopeptides containing phosphoserine in the +3 position were readily phosphorylated. In contrast, corresponding phosphothreonine-containing peptides were very poorly phosphorylated. These results imply that prior phosphorylation of substrate proteins on serine, but not threonine residues, may be important in regulating their phosphorylation by casein kinase II.

【 授权许可】

Unknown