Premium
A novel nuclear 42‐kDa casein kinase identified in Chironomus tentans
Author(s) -
Stigare J.,
Kovacs J.,
Buddelmeijer N.,
Egyhazi E.
Publication year - 1992
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(92)81498-b
Subject(s) - casein kinase 2, alpha 1 , casein kinase 2 , casein kinase 1 , phosvitin , microbiology and biotechnology , biochemistry , phosphoprotein , autophosphorylation , mitogen activated protein kinase kinase , protein kinase a , kinase , biology , cyclin dependent kinase 9 , map2k7 , cyclin dependent kinase 2 , casein , cyclin dependent kinase 7 , phosphorylation , chemistry
We have purified and characterised an apparently novel nuclear 42‐kDa casein kinase from epithelial cells of Chironomus tentans which comigrates with a phosphoprotein associated with transcriptionally active salivary gland genes. The protein kinase promotes phosphorylation of casein and phosvitin, using either ATP or GTP as phosphate donors, and undergoes autophosphorylation. The casein kinase activity of the 42‐kDa protein sensitive to heparin, 5,6‐dichloro‐1‐β‐ d ‐ribofuranosylbezimidazole (DRB), spermine and spermidine indicating that it is a novel enzyme with similar but not identical properties to casein kinase II or nuclear protein kinase NII.