Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractOnline analysis of volatile organic compound emissions from Sitka spruce (Picea sitchensis)    Next Abstract"Production of the rat complement regulator, Crry, as an active soluble protein in Pichia pastoris" »

Proc Natl Acad Sci U S A


Title:"RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins"
Author(s):He B; Chen P; Chen SY; Vancura KL; Michaelis S; Powers S;
Address:"Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854"
Journal Title:Proc Natl Acad Sci U S A
Year:1991
Volume:88
Issue:24
Page Number:11373 - 11377
DOI: 10.1073/pnas.88.24.11373
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"In the yeast Saccharomyces cerevisiae, mutations in either of two unlinked genes, RAM1 or RAM2, abolish the farnesyltransferase activity responsible for prenylation of Ras proteins and the a-factor mating pheromone. Here we report that the function of RAM1 and RAM2 genes is required for the membrane localization of Ras proteins and a-factor. The RAM2 gene was sequenced and can encode a 38-kDa protein. We examined the functional interaction of RAM2 and RAM1 by expressing the genes in Escherichia coli. Extracts derived from an E. coli strain that coexpressed RAM1 and RAM2 efficiently farnesylated a-factor peptide and Ras protein substrates. In contrast, extracts derived from E. coli strains that expressed either RAM gene alone were devoid of activity; however, when the latter extracts were mixed, protein farnesyltransferase activity was reconstituted. These results indicate that the yeast farnesyl-protein transferase is comprised of Ram1 and Ram2 polypeptides. Although Ram1 is a component of the enzyme, disruption of the RAM1 gene in yeast was not lethal, indicating that the Ram1-Ram2 farnesyltransferase is not essential for viability. In contrast, disruption of RAM2 was lethal, suggesting that Ram2 has an essential function in addition to its role with Ram1 in protein farnesylation"
Keywords:"*Alkyl and Aryl Transferases Amino Acid Sequence Base Sequence Escherichia coli/genetics Fungal Proteins/*metabolism GTP-Binding Proteins/metabolism *Genes, Fungal Mating Factor Molecular Sequence Data Mutagenesis, Insertional Peptides/*metabolism Pheromo;"
Notes:"MedlineHe, B Chen, P Chen, S Y Vancura, K L Michaelis, S Powers, S eng GM41223/GM/NIGMS NIH HHS/ GM41258/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1991/12/15 Proc Natl Acad Sci U S A. 1991 Dec 15; 88(24):11373-7. doi: 10.1073/pnas.88.24.11373"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 06-07-2024