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 Abstract"Remediation of the Wells G & H Superfund Site, Woburn, Massachusetts"    Next Abstract"Transcriptional profiling of Saccharomyces cerevisiae T2 cells upon exposure to hardwood spent sulphite liquor: comparison to acetic acid, furfural and hydroxymethylfurfural" »

Biochim Biophys Acta


Title:Role of extracellular charged amino acids in the yeast alpha-factor receptor
Author(s):Bajaj A; Connelly SM; Gehret AU; Naider F; Dumont ME;
Address:"Department of Biochemistry and Biophysics, P.O. Box 712, University of Rochester, School of Medicine and Dentistry, Rochester, NY 14642, USA"
Journal Title:Biochim Biophys Acta
Year:2007
Volume:20070217
Issue:6
Page Number:707 - 717
DOI: 10.1016/j.bbamcr.2007.02.002
ISSN/ISBN:0006-3002 (Print) 0006-3002 (Linking)
Abstract:"The yeast pheromone receptor, Ste2p, is a G protein coupled receptor that initiates cellular responses to alpha-mating pheromone, a 13 residue peptide that carries a net positive charge at physiological pH. We have examined the role of extracellular charged groups on the receptor in response to the pheromone. Substitutions of Asn or Ala for one extracellular residue, Asp275, affected both pheromone binding and signaling, suggesting that this position interacts directly with ligand. The other seven extracellular acidic residues could be individually replaced by polar residues with no detectable effects on receptor function. However, substitution of Ala for each of these seven residues resulted in impairment of signaling without affecting pheromone binding, implying that the polar nature of these residues promotes receptor activation. In contrast, substitution of Ala for each of the six positively charged residues at the extracellular surface of Ste2p did not affect signaling"
Keywords:"Amino Acid Substitution Amino Acids, Basic/genetics/*metabolism Aspartic Acid/genetics/*metabolism Mating Factor Mutation, Missense Peptides/genetics/metabolism Protein Binding/physiology Receptors, G-Protein-Coupled/genetics/*metabolism Receptors, Mating;"
Notes:"MedlineBajaj, Anshika Connelly, Sara M Gehret, Austin U Naider, Fred Dumont, Mark E eng R01 GM059357/GM/NIGMS NIH HHS/ GM59357/GM/NIGMS NIH HHS/ R01 GM022086-30/GM/NIGMS NIH HHS/ R01 GM022086/GM/NIGMS NIH HHS/ R01 GM059357-07/GM/NIGMS NIH HHS/ GM22086/GM/NIGMS NIH HHS/ R01 GM059357-06/GM/NIGMS NIH HHS/ R56 GM022086/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Netherlands 2007/04/17 Biochim Biophys Acta. 2007 Jun; 1773(6):707-17. doi: 10.1016/j.bbamcr.2007.02.002. Epub 2007 Feb 17"

 
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 17-11-2024