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 AbstractMolecular determinants of bioactivity of the Saccharomyces cerevisiae lipopeptide mating pheromone    Next AbstractDisruption of the fifth melanocortin receptor alters the urinary excretion of aggression-modifying pheromones in male house mice »

Microbiol Rev


Title:Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation
Author(s):Caldwell GA; Naider F; Becker JM;
Address:"Department of Microbiology, University of Tennessee, Knoxville 37996-0845, USA"
Journal Title:Microbiol Rev
Year:1995
Volume:59
Issue:3
Page Number:406 - 422
DOI: 10.1128/mr.59.3.406-422.1995
ISSN/ISBN:0146-0749 (Print) 0146-0749 (Linking)
Abstract:"In a variety of fungal species, mating between haploid cells is initiated by the action of peptide pheromones. The identification and characterization of several fungal pheromones has revealed that they have common structural features classifying them as lipopeptides. In the course of biosynthesis, these pheromones undergo a series of posttranslational processing events prior to export. One common modification is the attachment of an isoprenoid group to the C terminus of the pheromone precursor. Genetic and biochemical investigations of this biosynthetic pathway have led to the elucidation of genes and enzymes which are responsible for isoprenylation of other polypeptides including the nuclear lamins, several vesicular transport proteins, and the oncogene product Ras. The alpha-factor of Saccharomyces cerevisiae serves as a model for studying the biosynthesis, export, and bioactivity of lipopeptide pheromones. In addition to being isoprenylated with a farnesyl group, the alpha-factor is secreted by a novel peptide export pathway utilizing a yeast homolog of the mammalian multidrug resistance P-glycoprotein. The identification of putative lipopeptide-encoding loci within other fungi, including the human immunodeficiency virus-associated opportunistic pathogen Cryptococcus neoformans and the plant pathogen Ustilago maydis, has stimulated much interest in understanding possible roles for pheromones in fungal proliferation and pathogenicity. Knowledge of variations within the processing, export, and receptor-mediated signal transduction pathways associated with different fungal lipopeptide pheromones will continue to provide insights into similar mechanisms which exist in higher eukaryotes"
Keywords:Amino Acid Sequence Fungal Proteins/biosynthesis/chemistry/genetics/*physiology Fungi/*physiology Genetic Variation Lipoproteins/biosynthesis/chemistry/genetics/*physiology Molecular Sequence Data Pheromones/biosynthesis/chemistry/genetics/*physiology Pro;
Notes:"MedlineCaldwell, G A Naider, F Becker, J M eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ GM-46520/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. Review 1995/09/01 Microbiol Rev. 1995 Sep; 59(3):406-22. doi: 10.1128/mr.59.3.406-422.1995"

 
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 16-11-2024