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 AbstractFast Eruption Desorption Ionization for Mass Spectrometric Analysis    Next Abstract"Distributions and source apportionment of ambient volatile organic compounds in Beijing city, China" »

Plant Physiol


Title:Arabidopsis vegetative storage protein is an anti-insect acid phosphatase
Author(s):Liu Y; Ahn JE; Datta S; Salzman RA; Moon J; Huyghues-Despointes B; Pittendrigh B; Murdock LL; Koiwa H; Zhu-Salzman K;
Address:"Department of Entomology, Texas A&M University, College Station, TX 77843, USA"
Journal Title:Plant Physiol
Year:2005
Volume:20051028
Issue:3
Page Number:1545 - 1556
DOI: 10.1104/pp.105.066837
ISSN/ISBN:0032-0889 (Print) 1532-2548 (Electronic) 0032-0889 (Linking)
Abstract:"Indirect evidence previously suggested that Arabidopsis (Arabidopsis thaliana) vegetative storage protein (VSP) could play a role in defense against herbivorous insects. To test this hypothesis, other AtVSP-like sequences in Arabidopsis were identified through a Basic Local Alignment Search Tool search, and their transcriptional profiles were investigated. In response to methyl jasmonate application or phosphate starvation, AtVSP and AtVSP-like genes exhibited differential expression patterns, suggesting distinct roles played by each member. Arabidopsis VSP2 (AtVSP2), a gene induced by wounding, methyl jasmonate, insect feeding, and phosphate deprivation, was selected for bacterial expression and functional characterization. The recombinant protein exhibited a divalent cation-dependent phosphatase activity in the acid pH range. When incorporated into the diets of three coleopteran and dipteran insects that have acidic gut lumen, recombinant AtVSP2 significantly delayed development of the insects and increased their mortality. To further determine the biochemical basis of the anti-insect activity of the protein, the nucleophilic aspartic acid-119 residue at the conserved DXDXT signature motif was substituted by glutamic acid via site-directed mutagenesis. This single-amino acid alteration did not compromise the protein's secondary or tertiary structure, but resulted in complete loss of its acid phosphatase activity as well as its anti-insect activity. Collectively, we conclude that AtVSP2 is an anti-insect protein and that its defense function is correlated with its acid phosphatase activity"
Keywords:Acetates/pharmacology Acid Phosphatase/chemistry/genetics/*metabolism/pharmacology Amino Acid Sequence Animals Arabidopsis/enzymology/*metabolism Arabidopsis Proteins/chemistry/genetics/*metabolism/pharmacology Cyclopentanes/pharmacology Drosophila/drug e;
Notes:"MedlineLiu, Yilin Ahn, Ji-Eun Datta, Sumana Salzman, Ron A Moon, Jaewoong Huyghues-Despointes, Beatrice Pittendrigh, Barry Murdock, Larry L Koiwa, Hisashi Zhu-Salzman, Keyan eng Research Support, Non-U.S. Gov't 2005/11/01 Plant Physiol. 2005 Nov; 139(3):1545-56. doi: 10.1104/pp.105.066837. Epub 2005 Oct 28"

 
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 14-11-2024