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 AbstractIndoor air quality in green-renovated vs. non-green low-income homes of children living in a temperate region of US (Ohio)    Next Abstract"The effect of litter size on the growth, survival and behaviour of neonatal bulbectomised mice" »

Mol Cell Biol


Title:Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins
Author(s):Cooper A; Bussey H;
Address:"Department of Biology, McGill University, Quebec, Canada"
Journal Title:Mol Cell Biol
Year:1989
Volume:9
Issue:6
Page Number:2706 - 2714
DOI: 10.1128/mcb.9.6.2706-2714.1989
ISSN/ISBN:0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:"We have identified and partially characterized the Saccharomyces cerevisiae KEX1 gene product, Kex1p, to assess its role in processing secreted protein precursors. Anti-Kex1p antibodies identified a 113-kilodalton protein that was absent in cells in which the KEX1 gene has been disrupted and that was more abundant in cells overexpressing the KEX1 gene. Kex1p was found to be a membrane-associated glycoprotein with N-linked carbohydrate. The N-linked oligosaccharide(s) was modified in a progressive manner after synthesis, causing the glycoprotein to slowly increase in mass to 115 kilodaltons. After a Kex2p-mediated cleavage event at specific pairs of basic amino acids, alpha-factor and K1 killer toxin precursors have COOH-terminal dibasic residue extensions and require a carboxypeptidase B-like enzyme to process the precursors to maturity. A carboxypeptidase activity, with apparent specificity for basic amino acids, was detected in KEX1 cells. Disruption of the KEX1 gene abolished this activity, while overexpression of KEX1 increased it. Our results provide biochemical evidence consistent with earlier genetic work, that KEX1 encodes a serine carboxypeptidase involved in the processing of precursors to secreted mature proteins"
Keywords:"Base Sequence Binding, Competitive Carboxypeptidases/*genetics/metabolism Cathepsin A Centrifugation Electrophoresis, Polyacrylamide Gel Fungal Proteins/*genetics/metabolism *Genes, Fungal Killer Factors, Yeast Mating Factor Membrane Proteins/genetics/met;"
Notes:"MedlineCooper, A Bussey, H eng Research Support, Non-U.S. Gov't 1989/06/01 Mol Cell Biol. 1989 Jun; 9(6):2706-14. doi: 10.1128/mcb.9.6.2706-2714.1989"

 
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