cAMP-dependent protein kinase fromDictyostelium discoideum

✍ Scribed by Veron, Michel ;Mutzel, Rupert ;Lacombe, Marie-Lise ;Simon, Marie-Noëlle ;Wallet, Valérie

• Book ID: 102819511
• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 834 KB
• Volume: 9
• Category: Article
• ISSN: 0192-253X
• DOI: 10.1002/dvg.1020090407

✦ Synopsis

The CAMP-dependent protein kinase (cAK) from Diciyosteliurn discoideurn is an enzyme composed of one catalytic and one regulatory subunit. Upon binding of CAMP, the holoenzyme dissociates to liberate free active catalytic subunits. The cAK is developmentally regulated, ranging from very little activity in vegetative cells to maximal expression in postaggregative cells. Although there is no immunological cross-reaction between the subunits of cAKs from Diciyosteliurn and from other organisms, they share several hiochemical properties. A complete cDNA for the regulatory subunit has been cloned and sequenced. Only one copy of the gene for the regulatory subunit is present per haploid genome. On the basis of the comparison of the structure of the cAK from Dicryosteliurn with its counterparts in yeast and higher eukaryotes, we propose a model for the evolution of cyclic-nucleotide-binding proteins.