ISSN:
1617-4623
Keywords:
Saccharomyces cerevisiae
;
cAMP-dependent protein kinase
;
Regulatory subunit
;
Site-directed mutagenesis
;
Phosphorylation site
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary 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, BCY1 Ala 145 (Ser145 to Ala), BCY1 His 143 (Arg143 to His) and BCY1 Asn 144, Ala 145 (Thr144 to Asn and Ser145 to Ala) complemented a bcy1 mutant, whereas BCY1 Gly 143 (Arg143 to Gly) did not. In addition, mutant, BCY1 Asn 144, Ala 145 exhibited a dominant coldsensitive 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00327191
Permalink
