Abstract
In the thermosensitive cdc25 start mutant of Saccharomyces cerevisiae, the regulation of adenylate cyclase by guanyl nucleotides was rapidly nullified when the enzyme was prepared from nonsynchronized cells shifted to the restrictive temperature. In agreement with previous in vivo complementation studies, this biochemical defect was fully suppressed by the expression of either the whole cloned CDC25 gene or its C-terminal portion. Moreover, membranes prepared from cdc25(Ts) cells grown at the permissive temperature evinced an altered regulation of adenylate cyclase by guanyl nucleotides. These results indicate that the CDC25 protein, together with RAS, is involved in the regulation of adenylate cyclase by guanyl nucleotides and raise the possibility that adenylate cyclase might form a ternary complex with RAS and CDC25.
MeSH Terms
Adenylyl Cyclases/metabolism
Cell Cycle
Enzyme Activation
Fungal Proteins/physiology
GTP-Binding Proteins/physiology
Genes, Fungal
Guanine Nucleotides/physiology
Membrane Proteins/physiology
Mutation
Saccharomyces cerevisiae/physiology
Temperature
Chemicals
Fungal Proteins
Guanine Nucleotides
Membrane Proteins
GTP-Binding Proteins
Adenylyl Cyclases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Daniel J
Department of Biochemistry, Weizmann Institute of Science, Rehovot, Israel.
Becker J M
Enari E
Levitzki A
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