Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila
Identifieur interne : 000788 ( Main/Exploration ); précédent : 000787; suivant : 000789Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila
Auteurs : Faisal Younus [Australie] ; Nicholas J. Fraser [Australie] ; Chris W. Coppin [Australie] ; Jian-Wei Liu [Australie] ; Galen J. Correy [Australie] ; Thomas Chertemps [France] ; Gunjan Pandey [Australie] ; Martine Maïbèche [France] ; Colin J. Jackson [Australie] ; John G. Oakeshott [Australie]Source :
- Scientific Reports [ 2045-2322 ] ; 2017.
Abstract
Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.
Url:
DOI: 10.1038/srep46188
PubMed: 28393888
PubMed Central: 5385555
Affiliations:
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Jackson</name><affiliation wicri:level="1"><nlm:aff id="a2"><institution>Research School of Chemistry, Australian National University</institution>, Canberra, ACT, 2601,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></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 wicri:level="1"><nlm:aff id="a1"><institution>CSIRO Land and Water, Black Mountain</institution>, Canberra, ACT, 2601,<country>Australia</country></nlm:aff><country xml:lang="fr">Australie</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Scientific Reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Carey, A F" uniqKey="Carey A">A. F. Carey</name></author><author><name sortKey="Carlson, J R" uniqKey="Carlson J">J. R. 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Han</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Australie</li><li>France</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Younus, Faisal" sort="Younus, Faisal" uniqKey="Younus F" first="Faisal" last="Younus">Faisal Younus</name></noRegion><name sortKey="Coppin, Chris W" sort="Coppin, Chris W" uniqKey="Coppin C" first="Chris W." last="Coppin">Chris W. Coppin</name><name sortKey="Correy, Galen J" sort="Correy, Galen J" uniqKey="Correy G" first="Galen J." last="Correy">Galen J. Correy</name><name sortKey="Fraser, Nicholas J" sort="Fraser, Nicholas J" uniqKey="Fraser N" first="Nicholas J." last="Fraser">Nicholas J. Fraser</name><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J." last="Jackson">Colin J. Jackson</name><name sortKey="Liu, Jian Wei" sort="Liu, Jian Wei" uniqKey="Liu J" first="Jian-Wei" last="Liu">Jian-Wei Liu</name><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G." last="Oakeshott">John G. Oakeshott</name><name sortKey="Pandey, Gunjan" sort="Pandey, Gunjan" uniqKey="Pandey G" first="Gunjan" last="Pandey">Gunjan Pandey</name><name sortKey="Younus, Faisal" sort="Younus, Faisal" uniqKey="Younus F" first="Faisal" last="Younus">Faisal Younus</name></country><country name="France"><noRegion><name sortKey="Chertemps, Thomas" sort="Chertemps, Thomas" uniqKey="Chertemps T" first="Thomas" last="Chertemps">Thomas Chertemps</name></noRegion><name sortKey="Maibeche, Martine" sort="Maibeche, Martine" uniqKey="Maibeche M" first="Martine" last="Maïbèche">Martine Maïbèche</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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