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The catalytic subunit of Dictyostelium cAMP-dependent protein kinase: role of the N-terminal domain and of the C-terminal residues in catalytic activity and stability



The catalytic subunit of Dictyostelium cAMP-dependent protein kinase: role of the N-terminal domain and of the C-terminal residues in catalytic activity and stability



European Journal of Biochemistry 248(3): 820-826



The C subunit of Dictyostelium cAMP-dependent protein kinase (PKA) is unusually large (73 kDa) due to the presence of 330 amino acids N-terminal to the conserved catalytic core. The sequence following the core, including a C-terminal -Phe-Xaa-Xaa-Phe-COOH motif, is highly conserved. We have characterized the catalytic activity and stability of C subunits mutated in sequences outside the catalytic core and we have analyzed their ability to interact with the R subunit and with the heat-stable protein-kinase inhibitor PKI. Mutants carrying deletions in the N-terminal domain displayed little difference in their kinetic properties and retained their capacity to be inhibited by R subunit and by PKI. In contrast, the mutation of one or both of the phenylalanine residues in the C-terminal motif resulted in a decrease of catalytic activity and stability of the proteins. Inhibition by the R subunit or by PKI were however unaffected. Sequence-comparison analysis of other protein kinases revealed that a -Phe-Xaa-Xaa-Phe- motif is present in many Ser/Thr protein kinases, although its location at the very end of the polypeptide is a particular feature of the PKA family. We propose that the presence of this motif may serve to identify isoforms of protein kinases.

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Accession: 009547235

Download citation: RISBibTeXText

PMID: 9342234

DOI: 10.1111/j.1432-1033.1997.t01-2-00820.x


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