title: Functional analysis of the catalytic subunit of Dictyostelium PKA in vivo.
abstract: 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.
authors.affiliation: Unité de Régulation Enzymatique des Activités Cellulaires, Institut Pasteur, 25 rue du Dr. Roux, 75724, Paris Cedex 15, France.
authors.forename: H
authors.initials: H
authors.lastname: Dammann
authors.forename: F
authors.initials: F
authors.lastname: Traincard
authors.forename: C
authors.initials: C
authors.lastname: Anjard
authors.forename: M X
authors.initials: MX
authors.lastname: van Bemmelen
authors.forename: C
authors.initials: C
authors.lastname: Reymond
authors.forename: M
authors.initials: M
authors.lastname: Véron
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D017868:Cyclic AMP-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism*; D004023:Dictyostelium / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D017868:Cyclic AMP-Dependent Protein Kinases