J. Biochem, 1993, Vol. 114, No. 2 167-170
© 1993 Japanese Biochemical Society
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Requirement of Brain Extract for the Activity of Brain Calmodulin-Dependent Protein Kinase IV Expressed in Escherichia coli1
Department of Biochemistry, Asahikawa Medical College Asahikawa, Hokkaido 078
Calmodulin-dependent protein kinase IV (CaM-kinase IV) is a Ca2+-responsive multifunctional protein kinase which occurs abundantly in the brain. When cDNA for rat brain CaM-kinase IV was expressed in Escherichia coli, the enzyme was produced in a good yield, but it did not show significant activity. The inactive recombinant CaM-kinase IV was phosphorylated and became highly active on incubation with a rat brain extract in the presence of both Ca2+/calmodulin and ATP/Mg2+. The recombinant CaM-kinase IV-activating activity in brain was one to two orders of magnitude higher than that in the other tissues examined. These observations suggest that CaM-kinase IV may undergo a posttranslational modification, probably Ca2+/calmodulin-dependent phosphorylation by CaM-kinase IV kinase, before exhibiting activity in the central nervous system.
1 This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, by the Smoking Research Foundation, and by the Byotai Taisha Research Foundation.
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