Heterogeneity of the glutathione transferase genes encoding enzymes responsible for insecticide degradation in the housefly

Michael Syvanen, Zonghan Zhou, Jonathan Wharton, Claire Goldsbury, Alan Clark

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

One of the four glutathione-S-transferases (GST) that is overproduced in the insecticide-resistant Cornell-R strain of the housefly (Musca domestica) produces an activity that degrades the insecticide dimethyl parathion and conjugates glutathione to lindane. In earlier work, it was shown that the resistant Comell-R carries an amplification, probably a duplication, of one or more of its GST loci and that this amplification is directly related to resistance. Using polymerase chain reaction (PCR) amplification with genomic DNA, multiple copies of the gene encoding the parathion-degrading activity (called MdGst-3) were subcloned from both the ancestral, insecticide- susceptible strain BPM and from the insecticide-resistant Cornell-R. In BPM, three different MdGst-3 genes were identified while in Cornell-R, 12 different MdGst-3 sequences were found that, though closely related to ancestral genes, had diverged by a few nucleotides. This diversity in MdGst- 3 genomic sequences in Cornell-R is reflected in the expressed sequences, as sampled through a cDNA bank. Population heterozygosity cannot account for these multiple GST genes. We suggest that selection for resistance to insecticides has resulted in not only amplification of the MdGst-3 genes but also in the divergence of sequence between the amplified copies.

Original languageEnglish (US)
Pages (from-to)236-240
Number of pages5
JournalJournal of Molecular Evolution
Volume43
Issue number3
StatePublished - 1996

Fingerprint

Houseflies
Gene encoding
Insecticides
Glutathione Transferase
glutathione transferase
insecticide
Amplification
enzyme
amplification
Degradation
insecticides
degradation
Genes
gene
Parathion
Enzymes
enzymes
parathion
genes
genomics

Keywords

  • Enzymes
  • Glutathione transferase genes
  • Housefly
  • Insecticide degradation

ASJC Scopus subject areas

  • Genetics
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Genetics(clinical)
  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this

Heterogeneity of the glutathione transferase genes encoding enzymes responsible for insecticide degradation in the housefly. / Syvanen, Michael; Zhou, Zonghan; Wharton, Jonathan; Goldsbury, Claire; Clark, Alan.

In: Journal of Molecular Evolution, Vol. 43, No. 3, 1996, p. 236-240.

Research output: Contribution to journalArticle

Syvanen, Michael ; Zhou, Zonghan ; Wharton, Jonathan ; Goldsbury, Claire ; Clark, Alan. / Heterogeneity of the glutathione transferase genes encoding enzymes responsible for insecticide degradation in the housefly. In: Journal of Molecular Evolution. 1996 ; Vol. 43, No. 3. pp. 236-240.
@article{56909f2b888449a781edf762968cf2ff,
title = "Heterogeneity of the glutathione transferase genes encoding enzymes responsible for insecticide degradation in the housefly",
abstract = "One of the four glutathione-S-transferases (GST) that is overproduced in the insecticide-resistant Cornell-R strain of the housefly (Musca domestica) produces an activity that degrades the insecticide dimethyl parathion and conjugates glutathione to lindane. In earlier work, it was shown that the resistant Comell-R carries an amplification, probably a duplication, of one or more of its GST loci and that this amplification is directly related to resistance. Using polymerase chain reaction (PCR) amplification with genomic DNA, multiple copies of the gene encoding the parathion-degrading activity (called MdGst-3) were subcloned from both the ancestral, insecticide- susceptible strain BPM and from the insecticide-resistant Cornell-R. In BPM, three different MdGst-3 genes were identified while in Cornell-R, 12 different MdGst-3 sequences were found that, though closely related to ancestral genes, had diverged by a few nucleotides. This diversity in MdGst- 3 genomic sequences in Cornell-R is reflected in the expressed sequences, as sampled through a cDNA bank. Population heterozygosity cannot account for these multiple GST genes. We suggest that selection for resistance to insecticides has resulted in not only amplification of the MdGst-3 genes but also in the divergence of sequence between the amplified copies.",
keywords = "Enzymes, Glutathione transferase genes, Housefly, Insecticide degradation",
author = "Michael Syvanen and Zonghan Zhou and Jonathan Wharton and Claire Goldsbury and Alan Clark",
year = "1996",
language = "English (US)",
volume = "43",
pages = "236--240",
journal = "Journal of Molecular Evolution",
issn = "0022-2844",
publisher = "Springer New York",
number = "3",

}

TY - JOUR

T1 - Heterogeneity of the glutathione transferase genes encoding enzymes responsible for insecticide degradation in the housefly

AU - Syvanen, Michael

AU - Zhou, Zonghan

AU - Wharton, Jonathan

AU - Goldsbury, Claire

AU - Clark, Alan

PY - 1996

Y1 - 1996

N2 - One of the four glutathione-S-transferases (GST) that is overproduced in the insecticide-resistant Cornell-R strain of the housefly (Musca domestica) produces an activity that degrades the insecticide dimethyl parathion and conjugates glutathione to lindane. In earlier work, it was shown that the resistant Comell-R carries an amplification, probably a duplication, of one or more of its GST loci and that this amplification is directly related to resistance. Using polymerase chain reaction (PCR) amplification with genomic DNA, multiple copies of the gene encoding the parathion-degrading activity (called MdGst-3) were subcloned from both the ancestral, insecticide- susceptible strain BPM and from the insecticide-resistant Cornell-R. In BPM, three different MdGst-3 genes were identified while in Cornell-R, 12 different MdGst-3 sequences were found that, though closely related to ancestral genes, had diverged by a few nucleotides. This diversity in MdGst- 3 genomic sequences in Cornell-R is reflected in the expressed sequences, as sampled through a cDNA bank. Population heterozygosity cannot account for these multiple GST genes. We suggest that selection for resistance to insecticides has resulted in not only amplification of the MdGst-3 genes but also in the divergence of sequence between the amplified copies.

AB - One of the four glutathione-S-transferases (GST) that is overproduced in the insecticide-resistant Cornell-R strain of the housefly (Musca domestica) produces an activity that degrades the insecticide dimethyl parathion and conjugates glutathione to lindane. In earlier work, it was shown that the resistant Comell-R carries an amplification, probably a duplication, of one or more of its GST loci and that this amplification is directly related to resistance. Using polymerase chain reaction (PCR) amplification with genomic DNA, multiple copies of the gene encoding the parathion-degrading activity (called MdGst-3) were subcloned from both the ancestral, insecticide- susceptible strain BPM and from the insecticide-resistant Cornell-R. In BPM, three different MdGst-3 genes were identified while in Cornell-R, 12 different MdGst-3 sequences were found that, though closely related to ancestral genes, had diverged by a few nucleotides. This diversity in MdGst- 3 genomic sequences in Cornell-R is reflected in the expressed sequences, as sampled through a cDNA bank. Population heterozygosity cannot account for these multiple GST genes. We suggest that selection for resistance to insecticides has resulted in not only amplification of the MdGst-3 genes but also in the divergence of sequence between the amplified copies.

KW - Enzymes

KW - Glutathione transferase genes

KW - Housefly

KW - Insecticide degradation

UR - http://www.scopus.com/inward/record.url?scp=0029814515&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029814515&partnerID=8YFLogxK

M3 - Article

C2 - 8703089

AN - SCOPUS:0029814515

VL - 43

SP - 236

EP - 240

JO - Journal of Molecular Evolution

JF - Journal of Molecular Evolution

SN - 0022-2844

IS - 3

ER -