The molecular basis for the neofunctionalization of the juvenile hormone esterase duplication in Drosophila

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dc.contributor.authorHopkins, Davis
dc.contributor.authorRane, R.V.
dc.contributor.authorYounus, Faisal
dc.contributor.authorCoppin, C.W.
dc.contributor.authorPandey, Gunjan
dc.contributor.authorJackson, Colin
dc.contributor.authorOakeshott, J.G.
dc.date.accessioned2020-04-01T00:21:43Z
dc.date.issued2019
dc.date.updated2019-11-25T07:46:36Z
dc.description.abstractThe Drosophila melanogaster enzymes juvenile hormone esterase (DmJHE) and its duplicate, DmJHEdup, present ideal examples for studying the structural changes involved in the neofunctionalization of enzyme duplicates. DmJHE is a hormone esterase with precise regulation and highly specific activity for its substrate, juvenile hormone. DmJHEdup is an odorant degrading esterase (ODE) responsible for processing various kairomones in antennae. Our phylogenetic analysis shows that the JHE lineage predates the hemi/holometabolan split and that several duplications of JHEs have been templates for the evolution of secreted β-esterases such as ODEs through the course of insect evolution. Our biochemical comparisons further show that DmJHE has sufficient substrate promiscuity and activity against odorant esters for a duplicate to evolve a general ODE function against a range of mid-long chain food esters, as is shown in DmJHEdup. This substrate range complements that of the only other general ODE known in this species, Esterase 6. Homology models of DmJHE and DmJHEdup enabled comparisons between each enzyme and the known structures of a lepidopteran JHE and Esterase 6. Both JHEs showed very similar active sites despite low sequence identity (30%). Both ODEs differed drastically from the JHEs and each other, explaining their complementary substrate ranges. A small number of amino acid changes are identified that may have been involved in the early stages of the neofunctionalization of DmJHEdup. Our results provide key insights into the process of neofunctionalization and the structural changes that can be involved.en_AU
dc.description.sponsorshipThis work was supported by the Australian Research Council (Future Fellowship to C.J.J.; FT140101059), Australian Science and Industry Endowment Fund (C.J.J.; PF14-099), and by an Australian Government Research Training Program Scholarship (D.H.H.).en_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn0965-1748en_AU
dc.identifier.urihttp://hdl.handle.net/1885/202563
dc.language.isoen_AUen_AU
dc.publisherElsevieren_AU
dc.relationhttp://purl.org/au-research/grants/arc/FT140101059en_AU
dc.rights© 2019 Elsevier Ltden_AU
dc.sourceInsect Biochemistry and Molecular Biologyen_AU
dc.titleThe molecular basis for the neofunctionalization of the juvenile hormone esterase duplication in Drosophilaen_AU
dc.typeJournal articleen_AU
local.bibliographicCitation.lastpage18en_AU
local.bibliographicCitation.startpage10en_AU
local.contributor.affiliationHopkins, Davis, College of Science, ANUen_AU
local.contributor.affiliationRane, R.V., CSIROen_AU
local.contributor.affiliationYounus, Faisal, College of Science, ANUen_AU
local.contributor.affiliationCoppin, C.W., CSIRO Land & Water Flagshipen_AU
local.contributor.affiliationPandey, Gunjan, CSIRO (Land & Water Flagship)en_AU
local.contributor.affiliationJackson, Colin, College of Science, ANUen_AU
local.contributor.affiliationOakeshott, J.G., CSIRO Land & Water Flagshipen_AU
local.contributor.authoremailu4040768@anu.edu.auen_AU
local.contributor.authoruidHopkins, Davis, u4843722en_AU
local.contributor.authoruidYounus, Faisal, u4835789en_AU
local.contributor.authoruidJackson, Colin, u4040768en_AU
local.description.embargo2037-12-31
local.description.notesImported from ARIESen_AU
local.identifier.absfor030406 - Proteins and Peptidesen_AU
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciencesen_AU
local.identifier.ariespublicationu3102795xPUB944en_AU
local.identifier.citationvolume106en_AU
local.identifier.doi10.1016/j.ibmb.2019.01.001en_AU
local.identifier.scopusID2-s2.0-85060331273
local.identifier.uidSubmittedByu3102795en_AU
local.publisher.urlhttps://www.elsevier.com/en_AU
local.type.statusPublished Versionen_AU

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