The genetic basis of malathion resistance in housefly (Musca domestica L.) strains from Turkey

Date

2004-11-01

Author

Taskin, V
Kence, M

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

180
views

0
downloads

Organophosphate insecticide (parathion/diazinon) resistance in housefly ( Musca domestica L.) is associated with the change in carboxylesterase activity. The product of MdalphaE7 gene is probably playing a role in detoxification of xenobiotic esters. In our research, we have isolated, cloned and sequenced the MdalphaE7 gene from five different Turkish housefly strains. High doses of malathion ( 600 mug/fly) were applied in a laboratory environment for one year to Ceyhan1, Ceyhan2, Adana, and Ankara strains while no insecticide treatment was performed in the laboratory to Kirazli strain. Trp(251) --> Ser substitution was found in the product of MdalphaE7 gene in all malathion-resistant and Kirazli stocks. In addition, we checked the malathion carboxylesterase (MCE), percent remaining activities in acetylcholinesterase (AChE), glutathion-S-transferase (GST), and general esterase activities in all five strains used in this study. In comparing with universal standard sensitive control WHO, a high level of MCE and GST activities were observed while lower level of general esterase activities was detected in the tested strains. In addition, a higher percent remaining activities in AChE than WHO susceptible strain were observed in all malathion-resistant strains.

Subject Keywords

Genetics

URI

https://hdl.handle.net/11511/65042

Journal

RUSSIAN JOURNAL OF GENETICS

DOI

https://doi.org/10.1023/b:ruge.0000048663.17417.97

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

Development of a pcr-based specific method for the detection of aspergillus fumigatus by random cdna cloning Söyler, Alper; Ögel, Zümrüt Begüm; Department of Food Engineering (2004) Aspergillus fumigatus is a foodborne and airborne human pathogen which produces mycotoxins such as gliotoxin, helvolic acid, fumigallin, and fumigaclavin. The most common disease caused by A. fumigatus is aspergillosis, which is often fatal, especially among AIDS, cancer, and organ-transplant patients. In this study, random cDNA cloning was performed from a cDNA library of A. fumigatus (IMI 385708) constructed on ? ZAP Express. Some of these clones were selected according to their insert sizes and were furt...
Analysis of self-processing mechanism of galactose oxidase by site-directed mutagenesis and heterologous expression in Escherichia Coli Gençer, Burçak; Ögel, Zümrüt Begüm; Department of Biotechnology (2005) In this study, self-catalytic maturation of heterologously expressed pro-galactose oxidase was analysed in E.coli by altering some amino acids which were supposed to play a crucial role in pro-peptide removal. Galactose oxidase (GOase; EC 1.1.3.9) from Fusarium graminearum; having a molecular mass of 68kDa, is a monomeric, copper containing enzyme with an unusual thioether bond. The enzyme is produced as a precursor with an additional 8 amino acid pre- and a 17- amino acid pro-sequence at the N terminus. Pr...
Expression of recombinant acid protease (thermopsin) gene from Thermoplasma volcanium Koyuncu, Bilsev; Kocabıyık, Semra; Department of Biology (2006) Acid proteases, commonly known as aspartic proteases are degredative enzymes which catalyze the cleavage reaction of peptide bonds in proteins with a pH optimum in the acidic range (pH 3-4). Acid proteases have crucial roles in metabolism. Moreover, they are used in different fields of industry. Thermophilic microorganisms, especially archaea, gain special interest because of their thermal stability for both fundamental and industrial researches. Thermopsin is an extracellular acid protease and a member of ...
Cloning and expression of periplasmic (clp p-like) and membrane-bound serine protease genes of thermoplasma volcanium in escherichia coli Demirok, Burçak; Kocabıyık, Semra; Department of Biology (2006) Serine proteases are a family of proteases that utilize an activated serine residue in the substrate-binding pocket to catalytically hydrolyze peptide bonds. Enzymes which belong to this family, with a diverse array of metabolic and regulatory functions, play critical roles in cell physiology and pathology. ءClp̕s are a class of ATP dependent serine proteases which are composed of a protease (ClpP) and an ATPase (ClpA or ClpX) component. Their involvements in degrading proteins are especially implicated und...
Determination of malathion and diazinon resistance by sequencing the Md alpha E7 gene from Guatemala, Colombia, Manhattan, and Thailand housefly (Musca domestica L.) strains Taskin, V; Kence, M; Göçmen, Birşen (2004-04-01) Organophosphate (OP) insecticides (parathion/diazinon) resistance in housefly (Musca domestica L.) is associated with the change in carboxylesterase activity. The product of alphaE7 gene, which is a member of alpha-esterase gene cluster, is probably playing a role in detoxyfication of the xenobiotic esters. In parathion/diazinon resistant M. domestica species Gly(137) to Asp substitution was found in the active center of the product of alphaE7 gene. In malathion (an OP) resistant M. domestica strains Trp(25...

Citation Formats

V. Taskin and M. Kence, “The genetic basis of malathion resistance in housefly (Musca domestica L.) strains from Turkey,” RUSSIAN JOURNAL OF GENETICS, pp. 1215–1222, 2004, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/65042.