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The pde2 gene of Saccharomyces cerevisiae is allelic to rcal and encodes a phosphodiesterase which protects the cell from extracellullar cAMP
Author(s) -
Wilson Robert B.,
Renault Georges,
Jacquet Michel,
Tatchell Kelly
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81071-7
Subject(s) - saccharomyces cerevisiae , phosphodiesterase , gene , allele , genetics , biology , yeast , microbiology and biotechnology , biochemistry , enzyme
The high affinity cAMP phosphodiesterase, encoded by PDE2 , is an important component of the cAMP‐dependent protein kinase signaling system in Saccharomyces cerevisiae . An unexpected phenotype of pde2 mutants is sensitivity to external cAMP. This trait has been found independently for rca1 mutants and has been used to monitor the effects of cAMP on several biological processes. We demonstrate here that RCA1 is identical to PDE2 . Further analysis of the phenotype of pde2 deletions reveal that exogenously added cAMP results in an increase in the internal level of cAMP. This increase slows down the rate of cell division by increasing the length of the G 1 phase of the cell cycle and leads to increased cell volume. Also, cells with a disrupted PDE2 gene previously arrested by nutrient starvation rapidly lose thermotolerance when incubated with exogenous cAMP. From these observations we propose that a role of the PDE2‐encoded phosphodiesterase may be to help insulate the internal cAMP pools from the external environment. This protective role might also be important in other eukaryotic organisms where cAMP is a key second messenger.