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 AbstractVolatile organic compounds produced by Aureobasidium pullulans induce electrolyte loss and oxidative stress in Botrytis cinerea and Alternaria alternata    Next AbstractSimple analysis of volatile organic compounds (VOCs) in the atmosphere using passive samplers »

Mol Cell Biol


Title:Plant farnesyltransferase can restore yeast Ras signaling and mating
Author(s):Yalovsky S; Trueblood CE; Callan KL; Narita JO; Jenkins SM; Rine J; Gruissem W;
Address:"Department of Plant and Microbial Biology, University of California, Berkeley 94720, USA"
Journal Title:Mol Cell Biol
Year:1997
Volume:17
Issue:4
Page Number:1986 - 1994
DOI: 10.1128/MCB.17.4.1986
ISSN/ISBN:0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:"Farnesyltransferase (FTase) is a heterodimeric enzyme that modifies a group of proteins, including Ras, in mammals and yeasts. Plant FTase alpha and beta subunits were cloned from tomato and expressed in the yeast Saccharomyces cerevisiae to assess their functional conservation in farnesylating Ras and a-factor proteins, which are important for cell growth and mating. The tomato FTase beta subunit (LeFTB) alone was unable to complement the growth defect of ram1 delta mutant yeast strains in which the chromosomal FTase beta subunit gene was deleted, but coexpression of LeFTB with the plant alpha subunit gene (LeFTA) restored normal growth, Ras membrane association, and mating. LeFTB contains a novel 66-amino-acid sequence domain whose deletion reduces the efficiency of tomato FTase to restore normal growth to yeast ram1 delta strains. Coexpression of LeFTA and LeFTB in either yeast or insect cells yielded a functional enzyme that correctly farnesylated CaaX-motif-containing peptides. Despite their low degree of sequence homology, yeast and plant FTases shared similar in vivo and in vitro substrate specificities, demonstrating that this enzymatic modification of proteins with intermediates from the isoprenoid biosynthesis pathway is conserved in evolutionarily divergent eukaryotes"
Keywords:"*Alkyl and Aryl Transferases Amino Acid Sequence Animals Base Sequence Cloning, Molecular Conserved Sequence DNA Primers/genetics Farnesyltranstransferase Humans Solanum lycopersicum/enzymology/genetics Mating Factor Molecular Sequence Data Mutation Pepti;"
Notes:"MedlineYalovsky, S Trueblood, C E Callan, K L Narita, J O Jenkins, S M Rine, J Gruissem, W eng GM35827/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1997/04/01 Mol Cell Biol. 1997 Apr; 17(4):1986-94. doi: 10.1128/MCB.17.4.1986"

 
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 22-11-2024