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Mech Dev. 1998 Mar;72(1-2):149-57.

Functional analysis of the catalytic subunit of Dictyostelium PKA in vivo.

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Unité de Régulation Enzymatique des Activités Cellulaires, Institut Pasteur, 25 rue du Dr. Roux, 75724, Paris Cedex 15, France.


The catalytic subunit of the cAMP-dependent protein kinase (PKA) from Dictyostelium discoideum contains several domains, including an unusually long N-terminal extension preceding a highly conserved catalytic core. We transformed the aggregationless PkaC-null strain with several deletion constructs of both domains. Strains transformed with genes expressing catalytically-inactive polypeptides could not rescue development. Cotransformation with constructs encoding the N-terminal extension and the catalytic core, both unable to rescue development by themselves, yielded transformants able to proceed to late development. A 27-amino acid long hydrophobic region, immediately upstream of the catalytic core, was found indispensable for PKA function. A putative role of this sequence in the acquisition of the active conformation of the protein is discussed.

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