Journal of Biological Chemistry
Volume 277, Issue 35, 30 August 2002, Pages 31740-31752
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MECHANISMS OF SIGNAL TRANSDUCTION
Characterization of Saccharomyces cerevisiaeAcyl-protein Thioesterase 1, the Enzyme Responsible for G Protein α Subunit Deacylation in Vivo*

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Thioacylation is a reversible lipid modification of proteins that plays a role in the regulation of signal transduction. Acyl-protein thioesterase 1 (APT1) was identified as an enzyme capable of deacylating some thioacylated proteins in vitro. Saccharomyces cerevisiae open reading frame YLR118c encodes an enzyme homologous to Rattus norvegicus APT1. We demonstrate that the catalytic activity of the protein encoded by the yeast open reading frame is similar to that of rat APT1, and we designate the protein S. cerevisiae Apt1p. Yeasts bearing a disruption of the APT1 gene lack significant biochemically detectable acyl-protein thioesterase activity. They also fail to deacylate Gpa1p, the yeast Gα subunit, in metabolic radiolabeling studies. We conclude that native APT1 is the enzyme responsible for Gα subunit deacylation in S. cerevisiae and presumably other eukaryotes as well.

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Published, JBC Papers in Press, June 21, 2002, DOI 10.1074/jbc.M202505200

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This work was supported by National Institutes of Health Grant GM34497 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.