Identification of candidate odorant degrading gene/enzyme systems in the antennal transcriptome of Drosophila melanogaster.
Identifieur interne : 003400 ( PubMed/Corpus ); précédent : 003399; suivant : 003401Identification of candidate odorant degrading gene/enzyme systems in the antennal transcriptome of Drosophila melanogaster.
Auteurs : Faisal Younus ; Thomas Chertemps ; Stephen L. Pearce ; Gunjan Pandey ; Françoise Bozzolan ; Christopher W. Coppin ; Robyn J. Russell ; Martine Maïbèche-Coisne ; John G. OakeshottSource :
- Insect biochemistry and molecular biology [ 1879-0240 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Arthropod Antennae (metabolism), Base Sequence, Drosophila melanogaster (enzymology), Drosophila melanogaster (genetics), Enzymes (genetics), Enzymes (metabolism), Female, Gene Expression Profiling, Insect Proteins (metabolism), Male, Molecular Sequence Data, Odorants, Polymerase Chain Reaction, Reproduction (physiology), Sex Factors, Transcriptome.
- MESH :
- chemical , genetics : Enzymes.
- enzymology : Drosophila melanogaster.
- genetics : Drosophila melanogaster.
- metabolism : Arthropod Antennae, Enzymes, Insect Proteins.
- physiology : Reproduction.
- Animals, Base Sequence, Female, Gene Expression Profiling, Male, Molecular Sequence Data, Odorants, Polymerase Chain Reaction, Sex Factors, Transcriptome.
Abstract
The metabolism of volatile signal molecules by odorant degrading enzymes (ODEs) is crucial to the ongoing sensitivity and specificity of chemoreception in various insects, and a few specific esterases, cytochrome P450s, glutathione S-transferases (GSTs) and UDP-glycosyltransferases (UGTs) have previously been implicated in this process. Significant progress has been made in characterizing ODEs in Lepidoptera but very little is known about them in Diptera, including in Drosophila melanogaster, a major insect model. We have therefore carried out a transcriptomic analysis of the antennae of D. melanogaster in order to identify candidate ODEs. Virgin male and female and mated female antennal transcriptomes were determined by RNAseq. As with the Lepidoptera, we found that many esterases, cytochrome P450 enzymes, GSTs and UGTs are expressed in D. melanogaster antennae. As olfactory genes generally show selective expression in the antennae, a comparison to previously published transcriptomes for other tissues has been performed, showing preferential expression in the antennae for one esterase, JHEdup, one cytochrome P450, CYP308a1, and one GST, GSTE4. These largely uncharacterized enzymes are now prime candidates for ODE functions. JHEdup was expressed heterologously and found to have high catalytic activity against a chemically diverse group of known ester odorants for this species. This is a finding consistent with an ODE although it might suggest a general role in clearing several odorants rather than a specific role in clearing a particular odorant. Our findings do not preclude the possibility of odorant degrading functions for other antennally expressed esterases, P450s, GSTs and UGTs but, if so, they suggest that these enzymes also have additional functions in other tissues.
DOI: 10.1016/j.ibmb.2014.07.003
PubMed: 25038463
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Pearce</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia; Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Pandey, Gunjan" sort="Pandey, Gunjan" uniqKey="Pandey G" first="Gunjan" last="Pandey">Gunjan Pandey</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Bozzolan, Francoise" sort="Bozzolan, Francoise" uniqKey="Bozzolan F" first="Françoise" last="Bozzolan">Françoise Bozzolan</name><affiliation><nlm:affiliation>Université Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, F-75252 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Coppin, Christopher W" sort="Coppin, Christopher W" uniqKey="Coppin C" first="Christopher W" last="Coppin">Christopher W. Coppin</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J" last="Russell">Robyn J. Russell</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Maibeche Coisne, Martine" sort="Maibeche Coisne, Martine" uniqKey="Maibeche Coisne M" first="Martine" last="Maïbèche-Coisne">Martine Maïbèche-Coisne</name><affiliation><nlm:affiliation>Université Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, F-75252 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G" last="Oakeshott">John G. Oakeshott</name><affiliation><nlm:affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia. Electronic address: john.oakeshott@csiro.au.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Insect biochemistry and molecular biology</title><idno type="eISSN">1879-0240</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Arthropod Antennae (metabolism)</term><term>Base Sequence</term><term>Drosophila melanogaster (enzymology)</term><term>Drosophila melanogaster (genetics)</term><term>Enzymes (genetics)</term><term>Enzymes (metabolism)</term><term>Female</term><term>Gene Expression Profiling</term><term>Insect Proteins (metabolism)</term><term>Male</term><term>Molecular Sequence Data</term><term>Odorants</term><term>Polymerase Chain Reaction</term><term>Reproduction (physiology)</term><term>Sex Factors</term><term>Transcriptome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Enzymes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Drosophila melanogaster</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Drosophila melanogaster</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arthropod Antennae</term><term>Enzymes</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Reproduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Base Sequence</term><term>Female</term><term>Gene Expression Profiling</term><term>Male</term><term>Molecular Sequence Data</term><term>Odorants</term><term>Polymerase Chain Reaction</term><term>Sex Factors</term><term>Transcriptome</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The metabolism of volatile signal molecules by odorant degrading enzymes (ODEs) is crucial to the ongoing sensitivity and specificity of chemoreception in various insects, and a few specific esterases, cytochrome P450s, glutathione S-transferases (GSTs) and UDP-glycosyltransferases (UGTs) have previously been implicated in this process. Significant progress has been made in characterizing ODEs in Lepidoptera but very little is known about them in Diptera, including in Drosophila melanogaster, a major insect model. We have therefore carried out a transcriptomic analysis of the antennae of D. melanogaster in order to identify candidate ODEs. Virgin male and female and mated female antennal transcriptomes were determined by RNAseq. As with the Lepidoptera, we found that many esterases, cytochrome P450 enzymes, GSTs and UGTs are expressed in D. melanogaster antennae. As olfactory genes generally show selective expression in the antennae, a comparison to previously published transcriptomes for other tissues has been performed, showing preferential expression in the antennae for one esterase, JHEdup, one cytochrome P450, CYP308a1, and one GST, GSTE4. These largely uncharacterized enzymes are now prime candidates for ODE functions. JHEdup was expressed heterologously and found to have high catalytic activity against a chemically diverse group of known ester odorants for this species. This is a finding consistent with an ODE although it might suggest a general role in clearing several odorants rather than a specific role in clearing a particular odorant. Our findings do not preclude the possibility of odorant degrading functions for other antennally expressed esterases, P450s, GSTs and UGTs but, if so, they suggest that these enzymes also have additional functions in other tissues.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25038463</PMID><DateCreated><Year>2014</Year><Month>09</Month><Day>16</Day></DateCreated><DateCompleted><Year>2015</Year><Month>06</Month><Day>10</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0240</ISSN><JournalIssue CitedMedium="Internet"><Volume>53</Volume><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Insect biochemistry and molecular biology</Title><ISOAbbreviation>Insect Biochem. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Identification of candidate odorant degrading gene/enzyme systems in the antennal transcriptome of Drosophila melanogaster.</ArticleTitle><Pagination><MedlinePgn>30-43</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ibmb.2014.07.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0965-1748(14)00115-5</ELocationID><Abstract><AbstractText>The metabolism of volatile signal molecules by odorant degrading enzymes (ODEs) is crucial to the ongoing sensitivity and specificity of chemoreception in various insects, and a few specific esterases, cytochrome P450s, glutathione S-transferases (GSTs) and UDP-glycosyltransferases (UGTs) have previously been implicated in this process. Significant progress has been made in characterizing ODEs in Lepidoptera but very little is known about them in Diptera, including in Drosophila melanogaster, a major insect model. We have therefore carried out a transcriptomic analysis of the antennae of D. melanogaster in order to identify candidate ODEs. Virgin male and female and mated female antennal transcriptomes were determined by RNAseq. As with the Lepidoptera, we found that many esterases, cytochrome P450 enzymes, GSTs and UGTs are expressed in D. melanogaster antennae. As olfactory genes generally show selective expression in the antennae, a comparison to previously published transcriptomes for other tissues has been performed, showing preferential expression in the antennae for one esterase, JHEdup, one cytochrome P450, CYP308a1, and one GST, GSTE4. These largely uncharacterized enzymes are now prime candidates for ODE functions. JHEdup was expressed heterologously and found to have high catalytic activity against a chemically diverse group of known ester odorants for this species. This is a finding consistent with an ODE although it might suggest a general role in clearing several odorants rather than a specific role in clearing a particular odorant. Our findings do not preclude the possibility of odorant degrading functions for other antennally expressed esterases, P450s, GSTs and UGTs but, if so, they suggest that these enzymes also have additional functions in other tissues.</AbstractText><CopyrightInformation>Copyright © 2014 CSIRO. Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Younus</LastName><ForeName>Faisal</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia; Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chertemps</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, F-75252 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pearce</LastName><ForeName>Stephen L</ForeName><Initials>SL</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia; Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pandey</LastName><ForeName>Gunjan</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bozzolan</LastName><ForeName>Françoise</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, F-75252 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coppin</LastName><ForeName>Christopher W</ForeName><Initials>CW</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Russell</LastName><ForeName>Robyn J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maïbèche-Coisne</LastName><ForeName>Martine</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université Pierre et Marie Curie, Institut d'Ecologie et des Sciences de l'Environnement de Paris, F-75252 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oakeshott</LastName><ForeName>John G</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>CSIRO Ecosystems Sciences, Black Mountain, Clunies Ross Street, Canberra, ACT 0200, Australia. Electronic address: john.oakeshott@csiro.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>07</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Insect Biochem Mol Biol</MedlineTA><NlmUniqueID>9207282</NlmUniqueID><ISSNLinking>0965-1748</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004798">Enzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019476">Insect Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057506" MajorTopicYN="N">Arthropod Antennae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004331" MajorTopicYN="N">Drosophila melanogaster</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004798" MajorTopicYN="N">Enzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020869" MajorTopicYN="N">Gene Expression Profiling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019476" MajorTopicYN="N">Insect Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009812" MajorTopicYN="Y">Odorants</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012098" MajorTopicYN="N">Reproduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012737" MajorTopicYN="N">Sex Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D059467" MajorTopicYN="N">Transcriptome</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Antenna</Keyword><Keyword MajorTopicYN="N">Cytochrome P450</Keyword><Keyword MajorTopicYN="N">Esterase</Keyword><Keyword MajorTopicYN="N">Odorant degradation</Keyword><Keyword MajorTopicYN="N">Transcriptome</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>07</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>07</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25038463</ArticleId><ArticleId IdType="pii">S0965-1748(14)00115-5</ArticleId><ArticleId IdType="doi">10.1016/j.ibmb.2014.07.003</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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