Mutations of the adenylyl cyclase gene that block RAS function in Saccharomyces cerevisiae

Field, J., Xu, H. P., Michaeli, T., Ballester, R., Sass, P., Wigler, M. H., Colicelli, J. (January 1990) Mutations of the adenylyl cyclase gene that block RAS function in Saccharomyces cerevisiae. Science, 247 (4941). pp. 464-7. ISSN 0036-8075

URL: https://www.ncbi.nlm.nih.gov/pubmed/2405488
DOI: 10.1126/science.2405488

Abstract

The interaction between RAS proteins and adenylyl cyclase was studied by using dominant interfering mutations of adenylyl cyclase from the yeast Saccharomyces cerevisiae. RAS proteins activate adenylyl cyclase in this organism. A plasmid expressing a catalytically inactive adenylyl cyclase was found to interfere dominantly with this activation. The interfering region mapped to the leucine-rich repeat region of adenylyl cyclase, which is homologous to domains present in several other proteins and is thought to participate in protein-protein interactions.

Item Type: Paper
Additional Information:
Uncontrolled Keywords: Adenylate Cyclase genetics metabolism Codon Deoxyribonucleases Type II Site-Specific Escherichia coli genetics Fungal Proteins metabolism Genes, Fungal Leucine Mutation Plasmids Repetitive Sequences, Nucleic Acid Saccharomyces cerevisiae enzymology genetics Sequence Homology Nucleic Acid Transformation Genetic ras Proteins
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 characterization
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: 26 January 1990
Date Deposited: 13 Apr 2012 20:15
Last Modified: 18 Nov 2016 17:19
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26183

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