Abstract
Ras proteins undergo a series of posttranslational modifications that are critical for their cellular function. These modifications are necessary to anchor Ras proteins to the membrane. Yeast Ras2 proteins were purified with various degrees of modification and examined for their ability to activate their effector, adenylyl cyclase. The farnesylated intermediate form of Ras2 had more than 100 times higher affinity for adenylyl cyclase than for the unprocessed form. The subsequent palmitoylation reaction had little effect. In contrast, palmitoylation was required for efficient membrane localization of the Ras2 protein. These results indicate the importance of farnesylation in the interaction of Ras2 with its effector.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenylyl Cyclases / genetics
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Adenylyl Cyclases / isolation & purification
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Adenylyl Cyclases / metabolism*
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Line
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Cell Membrane / enzymology
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation
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Fungal Proteins / genetics
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Fungal Proteins / isolation & purification
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Fungal Proteins / metabolism*
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GTP-Binding Proteins / genetics
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GTP-Binding Proteins / metabolism*
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Genes, Fungal
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Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
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Insecta
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Kinetics
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Molecular Sequence Data
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Molecular Weight
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Oligodeoxyribonucleotides
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Palmitic Acid
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Palmitic Acids / metabolism
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Protein Binding
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Protein Processing, Post-Translational*
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Transfection
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ras Proteins*
Substances
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Fungal Proteins
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Oligodeoxyribonucleotides
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Palmitic Acids
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Palmitic Acid
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Guanosine 5'-O-(3-Thiotriphosphate)
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GTP-Binding Proteins
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RAS2 protein, S cerevisiae
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ras Proteins
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Adenylyl Cyclases