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

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Abstract
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.

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