Biochemical evidence that the N‐terminal segments of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2

FEBS Letters

Pinna, Lorenzo A²  Ghisellini, Paola¹  Sarno, Stefania²  Marin, Oriano²  Meggio, Flavio² 

[1]Istituto di Biofisica, Università di Genova, Corso Europa 30, 16132 Genoa, Italy

[2]Dipartimento di Chimica Biologica and Centro per lo Studio delle Biomembrane del CNR, Università di Padova, viale G. Colombo 3, 35121 Padua, Italy

关键词: Protein kinase CK2;    CK2 regulation;    Casein kinase II;    CK2 mutant;    Protein phosphorylation;    CDK;    cyclin dependent protein kinase;    Fmoc;    9-fluorenylmethoxycarbonyl;    HBTU;    2-(1H-benzotriazol-1-yl)-1;    1;    3;    3-tetramethyluronium hexafluorophosphate;    HOBt;    1-hydroxybenzotriazole;    HPLC;    high performance liquid chromatography;   

DOI  :  10.1016/S0014-5793(98)01516-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The concept that the amino-terminal segment plays a role in conferring high basal activity to protein kinase CK2 α subunit has been validated by generating two mutants (Y26F and Δ2–6) which are defective both in catalytic activity and in thermal stability. The additional finding that the activity of the two mutants is fully restored upon association with the regulatory β subunit, in conjunction with the observation that synthetic peptides reproducing the N-terminal segment (1–30) and the activation loop (175–201) of CK2α counteract the functional effects of the C-terminal domain of the β subunit, is consistent with a mechanism of activation of CK2 where the N-terminal domain of α and the C-terminal domain of β play interchangeable roles.

【 授权许可】

Unknown