Mutant regulatory subunit of 3',5'-cAMP-dependent protein kinase of yeast Saccharomyces cerevisiae.
Four mutants with amino acid substitution(s) at or near the putative phosphorylation site (Arg142 Arg143 Thr144 Ser145) of the regulatory subunit of cAMP-dependent protein kinase were obtained by site-directed mutagenesis. Three mutants, BCY1A1a145 (Ser145 to Ala), BCY1His143 (Arg143 to His) and BCY1Asn144, Ala145 (Thr144 to Asn and Ser145 to Ala) complemented a bcy1 mutant, whereas BCY1Gly143 (Arg143 to Gly) did not. In addition, mutant, BCY1Asn144, Ala145 exhibited a dominant cold-sensitive phenotype, which can be most easily explained by the functional alteration of the regulatory subunit of cAMP-dependent protein kinase by the mutations. Analyses of these mutant genes revealed that phosphorylation of the regulatory subunit is not a prerequisite for the regulation of the cAMP-dependent protein kinase activity in responding to the cAMP level.
Yamano
S
S
Department of Fermentation Technology, Hiroshima University, Japan.
Tanaka
K
K
Matsumoto
K
K
Toh-e
A
A
D000242:Cyclic AMP / Q000502:physiology; D004252:DNA Mutational Analysis; D004271:DNA, Fungal / Q000235:genetics; D005800:Genes, Fungal; D010641:Phenotype; D011494:Protein Kinases / Q000235:genetics*; D011953:Receptors, Cyclic AMP / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000254:growth & development; D013489:Suppression, Genetic
D004271:DNA, Fungal; D011953:Receptors, Cyclic AMP; D000242:Cyclic AMP; D011494:Protein Kinases