Guanine nucleotide activation of, and competition between, RAS proteins from Saccharomyces cerevisiae

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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URL: https://www.ncbi.nlm.nih.gov/pubmed/3299060
DOI: 10.1128/MCB.7.6.2128

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
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: http://repository.cshl.edu/id/eprint/26180

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