Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins

Goodman, L. E., Judd, S. R., Farnsworth, C. C., Powers, S., Gelb, M. H., Glomset, J. A., Tamanoi, F. (December 1990) Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins. Proceedings of the National Academy of Sciences of the United States of America, 87 (24). pp. 9665-9. ISSN 0027-8424 (Print)0027-8424

URL: http://www.ncbi.nlm.nih.gov/pubmed/2124698

Abstract

Ras proteins are post-translationally modified by farnesylation. In the present investigation, we identified an activity in crude soluble extracts of yeast cells that catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to yeast RAS2 protein. RAS2 proteins having a C-terminal Cys-Ali-Ali-Xaa sequence (where Ali is an aliphatic amino acid and Xaa is the unspecified C-terminal amino acid) served as substrates for this reaction, whereas RAS2 proteins with an altered or deleted Cys-Ali-Ali-Xaa sequence did not. A yeast mutant, dpr1/ram1, originally isolated as a Ras-processing mutant was shown to be defective in farnesyltransferase activity. In addition, another mutant, ram2, also was defective in the transferase activity. These results demonstrate that at least two genes, DPR1/RAM1 and RAM2, are required for the farnesyltransferase activity in yeast.

Item Type: Paper
Uncontrolled Keywords: *Alkyl and Aryl Transferases Amino Acid Sequence Fungal Proteins/*genetics GTP-Binding Proteins/genetics Genes, Fungal Kinetics Molecular Sequence Data *Mutation Protein Processing, Post-Translational Saccharomyces cerevisiae/*genetics/metabolism *Saccharomyces cerevisiae Proteins Transferases/metabolism *ras Proteins
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Ras
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Powers lab
Depositing User: Matt Covey
Date: December 1990
Date Deposited: 26 Feb 2014 16:26
Last Modified: 26 Feb 2014 16:26
PMCID: PMC55233
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29519

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