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Volume 271, Number 31, Issue of August 2, 1996 pp. 18333-18336
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
Constitutively Active Adenylyl Cyclase Mutant Requires Neither G Proteins nor Cytosolic Regulators

(Received for publication, May 6, 1996, and in revised form, May 28, 1996)

From the Department of Biological Chemistry, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205

Receptor-mediated G protein-linked adenylyl cyclase systems are universal signal transducers. We exploited the essential role of this cascade in Dictyostelium development to screen for random mutations in the catalytic component, ACA. This enzyme is activated by G protein -subunits acting in concert with a novel cytosolic regulator, CRAC. By suppression of the CRAC-null phenotype, we isolated constitutively active versions of the enzyme that require neither exogenous stimuli nor internal regulators. One mutant displayed a 15-fold increase in its V_max. It harbors a single amino acid substitution (L394S) affecting a conserved residue located in the first cytoplasmic loop near the N-terminal hydrophobic domain of ACA. The screening procedure can be adapted for isolation of constitutive mutations in mammalian adenylyl cyclases.

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