Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae

Nikawa, J., Sass, P., Wigler, M. H. (October 1987) Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae. Molecular & Cellular Biology, 7 (10). pp. 3629-36. ISSN 0270-7306

URL: https://www.ncbi.nlm.nih.gov/pubmed/2824992
DOI: 10.1128/MCB.7.10.3629

Abstract

Saccharomyces cerevisiae contains two genes which encode cyclic AMP (cAMP) phosphodiesterase. We previously isolated and characterized PDE2, which encodes a high-affinity cAMP phosphodiesterase. We have now isolated the PDE1 gene of S. cerevisiae, which encodes a low-affinity cAMP phosphodiesterase. These two genes represent highly divergent branches in the evolution of phosphodiesterases. High-copy-number plasmids containing either PDE1 or PDE2 can reverse the growth arrest defects of yeast cells carrying the RAS2(Val-19) mutation. PDE1 and PDE2 appear to account for the aggregate cAMP phosphodiesterase activity of S. cerevisiae. Disruption of both PDE genes results in a phenotype which resembles that induced by the RAS2(Val-19) mutation. pde1- pde2- ras1- ras2- cells are viable.

Item Type: Paper
Uncontrolled Keywords: 3',5'-Cyclic-Nucleotide Phosphodiesterase genetics Amino Acid Sequence Base Sequence Cloning Molecular Cyclic AMP metabolism DNA Mutational Analysis DNA Restriction Enzymes diagnostic use Gene Expression Regulation Genes Fungal Heat Molecular Sequence Data Saccharomyces cerevisiae genetics
Subjects: organism description > yeast > Saccharomyces
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Wigler lab
Depositing User: CSHL Librarian
Date: October 1987
Date Deposited: 05 Apr 2012 16:04
Last Modified: 04 Nov 2016 20:44
PMCID: PMC368017
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26031

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