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 AbstractEnvironmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin    Next AbstractInteraction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action »

J Bacteriol


Title:"Interaction of alpha-agglutinin and a-agglutinin, Saccharomyces cerevisiae sexual cell adhesion molecules"
Author(s):Zhao H; Shen ZM; Kahn PC; Lipke PN;
Address:"Department of Biological Sciences and the Institute for Biomolecular Structure and Function, Hunter College of the City University of New York, New York, 10021, USA"
Journal Title:J Bacteriol
Year:2001
Volume:183
Issue:9
Page Number:2874 - 2880
DOI: 10.1128/JB.183.9.2874-2880.2001
ISSN/ISBN:0021-9193 (Print) 1098-5530 (Electronic) 0021-9193 (Linking)
Abstract:"alpha-Agglutinin and a-agglutinin are complementary cell adhesion glycoproteins active during mating in the yeast Saccharomyces cerevisiae. They bind with high affinity and high specificity: cells of opposite mating types are irreversibly bound by a few pairs of agglutinins. Equilibrium and surface plasmon resonance kinetic analyses showed that the purified binding region of alpha-agglutinin interacted similarly with purified a-agglutinin and with a-agglutinin expressed on cell surfaces. At 20 degrees C, the K(D) for the interaction was 2 x 10(-9) to 5 x 10(-9) M. This high affinity was a result of a very low dissociation rate ( approximately 2.6 x 10(-4) s(-1)) coupled with a low association rate (= 5 x 10(4) M(-1) s(-1)). Circular-dichroism spectroscopy showed that binding of the proteins was accompanied by measurable changes in secondary structure. Furthermore, when binding was assessed at 10 degrees C, the association kinetics were sigmoidal, with a very low initial rate. An induced-fit model of binding with substantial apposition of hydrophobic surfaces on the two ligands can explain the observed affinity, kinetics, and specificity and the conformational effects of the binding reaction"
Keywords:Agglutinins/*metabolism Cell Adhesion Molecules/*metabolism Fungal Proteins/*metabolism/pharmacokinetics Kinetics Mating Factor Peptides/*metabolism Protein Binding Recombinant Proteins/metabolism Saccharomyces cerevisiae/*metabolism *Saccharomyces cerevi;
Notes:"MedlineZhao, H Shen, Z M Kahn, P C Lipke, P N eng G12 RR003037/RR/NCRR NIH HHS/ 1R01-GM47176/GM/NIGMS NIH HHS/ RR-03037/RR/NCRR NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 2001/04/09 J Bacteriol. 2001 May; 183(9):2874-80. doi: 10.1128/JB.183.9.2874-2880.2001"

 
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 22-09-2024