Yeast bcy1 mutants with stationary phase-specific defects

• Published in: Current genetics Vol. 32; no. 2; pp. 83 - 92
• Main Authors: Peck, V.M, Fuge, E.K, Padilla, P.A, Gomez, M.A, Werner-Washburne, M
• Format: Journal Article
• Language: English
• Published: United States 01.08.1997
• Subjects: Acetates; Acetates - metabolism; Amino Acid Sequence; bcy1 gene; binding sites; Carbon; Carbon - metabolism; Cell Division; Cell Division - genetics; Cell Survival; Cell Survival - genetics; cyclic AMP; Cyclic AMP - metabolism; Cyclic AMP-Dependent Protein Kinases; Cyclic AMP-Dependent Protein Kinases - drug effects; Cyclic AMP-Dependent Protein Kinases - genetics; Cyclic AMP-Dependent Protein Kinases - metabolism; defects; drug effects; enzyme activity; Eosine I Bluish; Eosine I Bluish - pharmacology; genes; genetics; Glycogen; Glycogen - metabolism; growth & development; interphase; Isoenzymes; metabolism; Molecular Sequence Data; mutagenesis; Mutagenesis, Site-Directed; mutants; Mutation; Nitrogen; Nitrogen - metabolism; Peptides; Peptides - pharmacology; pharmacology; phenotype; Recombinant Proteins; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - drug effects; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - growth & development; viability
• ISSN: 0172-8083; 1432-0983
• DOI: 10.1007/s002940050251

Entry into the stationary phase requires the yeast BCY1 gene, which encodes the regulatory subunit of the cAMP-dependent protein kinase (cAPK). New bcy1 mutants, constructed by in vitro mutagenesis of the 3'-region encoding the cAMP-binding domains, were classified as early or late-acting mutants based on viability studies. The late-acting bcy1 mutants accumulated fewer stationary phase-specific Bcy1p isoforms and had decreased cAPK activity. This late-acting class is novel and dies after 7 days in culture, later than two previously reported stationary phase mutants, ubi4 and ard1.