FEBS Letters | |
Dissection of the dual function of the β‐subunit of protein kinase CK2 (‘casein kinase‐2’): a synthetic peptide reproducing the carboxyl‐terminal domain mimicks the positive but not the negative effects of the whole protein | |
Issinger, Olaf-G.2  Boldyreff, Brigitte2  Pinna, Lorenzo A.1  Marin, Oriano1  Meggio, Flavio1  | |
[1] Dipartimento di Chimica Biologica, CRIBI and CNR, Centro per lo Studio della Fisiologia Mitocondriale, Università di Padova, via Trieste 75, 35121 Padova, Italy;Institut für Humangenetik, Universität des Saarlandes, D-66421 Homburg, Germany | |
关键词: Protein kinase CK2; Casein kinase-2; Protein phosphorylation; Calmodulin phosphorylation; CK2 β-subunit; | |
DOI : 10.1016/0014-5793(95)00295-K | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The dual function of the regulatory β-subunit of protein kinase CK2 is highlighted by its ability to abolish calmodulin phosphorylation in contrast to its stimulatory effect on the phosphorylation of peptide substrates. Here we show that a synthetic peptide reproducing the C-terminal region of the β-subunit (β[170–215]) stimulates to a similar extent the phosphorylation of either the peptide substrate or calmodulin and also protects the catalytic α-subunit against thermal inactivation as efficiently as full-length β-subunit. These data show that the positive and negative functions of the β-subunit reside in physically separated domains and that the elements responsible for positive regulation are located in the C-terminal region.
【 授权许可】
Unknown
【 预 览 】
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RO201912020300960ZK.pdf | 477KB | download |