Differential activation of yeast adenylate cyclase by wild type and mutant RAS proteins

Broek, D., Samily, N., Fasano, O., Fujiyama, A., Tamanoi, F., Northup, J., Wigler, M. H. (1985) Differential activation of yeast adenylate cyclase by wild type and mutant RAS proteins. Cell, 41 (3). pp. 763-770.

URL: https://www.ncbi.nlm.nih.gov/pubmed/3891097
DOI: 10.1016/S0092-8674(85)80057-X

Abstract

Purified RAS proteins, whether derived from the yeast RAS1 or RAS2 or the human H-ras genes, activate yeast adenylate cyclase in the presence of guanine nucleotides. These results confirm the prediction of earlier genetic and biochemical data and for the first time provide a complete biochemical assay for RAS protein function. A biochemical difference is observed between the RAS2 and RAS2val19 proteins in their ability to activate adenylate cyclase after preincubation with GTP.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > RAS
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 > gene expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Wigler lab
Depositing User: CSHL Librarian
Date: 1985
Date Deposited: 19 Apr 2012 15:54
Last Modified: 18 Nov 2016 17:12
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26165

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