Field, J., Broek, D., Kataoka, T., Wigler, M. H. (1987) Guanine nucleotide activation of, and competition between, RAS proteins from Saccharomyces cerevisiae. Molecular & Cellular Biology, 7 (6). pp. 2128-2133.
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Abstract
In the yeast Saccharomyces cerevisae, yeast RAS proteins are potent activators of adenylate cyclase. In the present work we measured the activity of adenylate cyclase in membranes from Saccharomyces cerevisae which overexpress this enzyme. The response of the enzyme to added RAS2 proteins bound with various guanine nucleotides and their analogs suggests that RAS2 proteins are active in their GTP-bound form and are virtually inactive in their GDP-bound form. Also, active RAS2 protein is not inhibited by inactive RAS2, suggesting that the inactive form does not compete with the active form in binding to its effector.
Item Type: | Paper |
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Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > RAS organism description > yeast > Saccharomyces bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression |
CSHL Authors: | |
Communities: | CSHL labs > Wigler lab |
Depositing User: | CSHL Librarian |
Date: | 1987 |
Date Deposited: | 13 Apr 2012 21:07 |
Last Modified: | 04 Nov 2016 20:38 |
PMCID: | PMC365334 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/26180 |
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