Abstract
AlF4- has long been known to associate with and activate the GDP-bound alpha subunits of heterotrimeric G-proteins. Recently the small guanine nucleotide binding protein Ras has also been shown to associate with AlF4- in the presence of stoichiometric amounts of its GTPase activating protein (GAP). Here we present the isolation of a stable Ras x GDP- x AlF4- x GAP ternary complex by gel filtration. In addition, we generalise the association of AlF4- with the small GTP-binding proteins by demonstrating ternary complex formation for the Cdc42, Rap and Ran proteins in the presence of their respective GAP proteins.
MeSH terms
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Aluminum Compounds / metabolism*
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Cell Cycle Proteins / isolation & purification
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Cell Cycle Proteins / metabolism
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Chromatography, Gel
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Cloning, Molecular
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Escherichia coli
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Fluorides / metabolism*
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GTP Phosphohydrolases / metabolism
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GTP-Binding Proteins / isolation & purification
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GTP-Binding Proteins / metabolism*
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GTPase-Activating Proteins
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Nuclear Proteins / isolation & purification
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Nuclear Proteins / metabolism
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Protein Binding
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Proteins / isolation & purification
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Proteins / metabolism*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
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ran GTP-Binding Protein
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rap GTP-Binding Proteins
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ras GTPase-Activating Proteins
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ras Proteins / isolation & purification
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ras Proteins / metabolism*
Substances
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Aluminum Compounds
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Cell Cycle Proteins
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GTPase-Activating Proteins
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Nuclear Proteins
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Proteins
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Recombinant Proteins
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ras GTPase-Activating Proteins
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tetrafluoroaluminate
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GTP Phosphohydrolases
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GTP-Binding Proteins
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cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
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ran GTP-Binding Protein
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rap GTP-Binding Proteins
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ras Proteins
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Fluorides