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"A subtilisin-like protein from soybean contains an embedded, cryptic signal that activates defense-related genes"    Next AbstractSynthesis and absolute configuration of multistriatin »

Curr Protein Pept Sci


Title:"Systemin, hydroxyproline-rich systemin and the induction of protease inhibitors"
Author(s):Pearce G;
Address:"Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA. pearce940@gmail.com"
Journal Title:Curr Protein Pept Sci
Year:2011
Volume:12
Issue:5
Page Number:399 - 408
DOI: 10.2174/138920311796391106
ISSN/ISBN:1875-5550 (Electronic) 1389-2037 (Linking)
Abstract:"Systemin, an 18-amino acid signaling peptide isolated from tomato leaves, has been found to be an integral component of the jasmine acid signaling pathway, leading to the synthesis of protease inhibitors (PIs). The discovery of systemin has led to a search for other peptide signals involved in defense in the Solanaceae and in other plant families. A new class of peptides having similar signaling properties but little sequence homology to systemin have been found and termed hydroxyproline-rich glycopeptide systemins (HypSys). These small (18-20 amino acids) glycopeptides, like systemin, are derived from larger precursor proteins (proHypSys) and until recently were thought to function only in protection from herbivore attack. However, HypSys peptides isolated from petunia induced the defensin gene, known for its involvement in pathogen defense. More recently, a HypSys glycopeptide was isolated from sweet potato, a member of the Convolvulaceae family and found to induce the sporamin gene which codes for the major storage protein in tubers with trypsin inhibitor activity. These recent discoveries expand the function and range of the HypSys family of glycopeptides and establish these unique inducible signaling molecules as potential components of defense pathways throughout the Eudicots. Herein we review the signaling and structural properties of systemin and the HypSys glycopeptides and their roles in the induction of PIs"
Keywords:"Cyclopentanes/metabolism Gene Expression Regulation, Plant Hydroxyproline/*chemistry Oxylipins/metabolism Peptides/*chemistry/genetics/*metabolism Plant Proteins/*chemistry/genetics/*metabolism Plants/enzymology/metabolism Protease Inhibitors/*metabolism;"
Notes:"MedlinePearce, Gregory eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review United Arab Emirates 2011/03/23 Curr Protein Pept Sci. 2011 Aug; 12(5):399-408. doi: 10.2174/138920311796391106"

 
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 26-12-2024