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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
Author(s) -
Marin Oriano,
Meggio Flavio,
Boldyreff Brigitte,
Issinger Olaf-G.,
Pinna Lorenzo A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00295-k
Subject(s) - protein subunit , phosphorylation , peptide , protein kinase a , casein kinase 2 , kinase , biochemistry , calmodulin , chemistry , microbiology and biotechnology , biology , mitogen activated protein kinase kinase , enzyme , gene
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.