Mutant regulatory subunit of 3',5'-cAMP-dependent protein kinase of yeast Saccharomyces cerevisiae |
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| Authors: | Shigeyuki Yamano Kazuma Tanaka Kunihiro Matsumoto and Akio Toh-e |
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| Institution: | (1) Department of Fermentation Technology, Hiroshima University, Shitami, Saijo, 724 Higashihiroshima, Japan;(2) DNAX Research Institute of Molecular and Cellular Biology, 94304-1104 Palo Alto, CA, USA;(3) Present address: Kirin Brewery Co. Ltd., 1-2-2 Soja-cho, 371 Maebashi-shi, Japan |
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| Abstract: | 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. |
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| Keywords: | Saccharomyces cerevisiae cAMP-dependent protein kinase Regulatory subunit Site-directed mutagenesis Phosphorylation site |
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