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J. Biol. Chem., Vol. 265, Issue 6, 3048-3053, Feb, 1990
SA Orellana and GS McKnight
The S49 mouse lymphoma mutant cell line Kin- is resistant to the cytotoxic
effects of elevated cAMP levels, has no detectable cAMP- dependent protein
kinase activity, and has depressed levels of cAMP- binding regulatory
subunits. We demonstrate that although the Kin- cell line lacks detectable
catalytic subunit protein, these cells express wild-type levels of mRNA for
both C alpha and C beta catalytic subunit isoforms. Translation of C alpha
mRNA appears to be normal in the Kin- cell, based on the observation that C
alpha mRNA associates with large polyribosomes in both wild-type and Kin-
cells. We cloned the C alpha cDNA from Kin- cells and show that its
transient expression in another cell type leads to activation of a
cAMP-sensitive luciferase reporter gene, suggesting that functional C alpha
protein is made. In addition to having catalytic activity, the C alpha
subunit from Kin- cells is inhibited in the presence of mouse RI alpha
regulatory subunit, indicating that formation of the holoenzyme complex is
normal. We suggest that the mutation responsible for the Kin- phenotype is
in a cellular component that directly or indirectly causes Kin- catalytic
subunit protein to be degraded rapidly.
The S49 Kin- cell line transcribes and translates a functional mRNA coding for the catalytic subunit of cAMP-dependent protein kinase
Department of Pharmacology, University of Washington, Seattle 98195.
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