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Two fatty acyl reductases involved in moth pheromone biosynthesis

Antony, Binu LU ; Ding, Baojian LU ; Moto, Ken'Ichi; Aldosari, Saleh A. and Aldawood, Abdulrahman S. (2016) In Scientific Reports 6.
Abstract

Fatty acyl reductases (FARs) constitute an evolutionarily conserved gene family found in all kingdoms of life. Members of the FAR gene family play diverse roles, including seed oil synthesis, insect pheromone biosynthesis, and mammalian wax biosynthesis. In insects, FAR genes dedicated to sex pheromone biosynthesis (pheromone-gland-specific fatty acyl reductase, pgFAR) form a unique clade that exhibits substantial modifications in gene structure and possesses unique specificity and selectivity for fatty acyl substrates. Highly selective and semi-selective 'single pgFARs' produce single and multicomponent pheromone signals in bombycid, pyralid, yponomeutid and noctuid moths. An intriguing question is how a 'single reductase' can direct... (More)

Fatty acyl reductases (FARs) constitute an evolutionarily conserved gene family found in all kingdoms of life. Members of the FAR gene family play diverse roles, including seed oil synthesis, insect pheromone biosynthesis, and mammalian wax biosynthesis. In insects, FAR genes dedicated to sex pheromone biosynthesis (pheromone-gland-specific fatty acyl reductase, pgFAR) form a unique clade that exhibits substantial modifications in gene structure and possesses unique specificity and selectivity for fatty acyl substrates. Highly selective and semi-selective 'single pgFARs' produce single and multicomponent pheromone signals in bombycid, pyralid, yponomeutid and noctuid moths. An intriguing question is how a 'single reductase' can direct the synthesis of several fatty alcohols of various chain lengths and isomeric forms. Here, we report two active pgFARs in the pheromone gland of Spodoptera, namely a semi-selective, C14:acyl-specific pgFAR and a highly selective, C16:acyl-specific pgFAR, and demonstrate that these pgFARs play a pivotal role in the formation of species-specific signals, a finding that is strongly supported by functional gene expression data. The study envisages a new area of research for disclosing evolutionary changes associated with C14 - and C16 -specific FARs in moth pheromone biosynthesis.

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publication status
published
subject
in
Scientific Reports
volume
6
publisher
Nature Publishing Group
external identifiers
  • scopus:84978890787
  • wos:000379746500001
ISSN
2045-2322
DOI
10.1038/srep29927
language
English
LU publication?
yes
id
2856af90-28c5-4e11-909f-0b39efb35a83
date added to LUP
2017-01-12 11:59:28
date last changed
2017-10-01 05:28:43
@article{2856af90-28c5-4e11-909f-0b39efb35a83,
  abstract     = {<p>Fatty acyl reductases (FARs) constitute an evolutionarily conserved gene family found in all kingdoms of life. Members of the FAR gene family play diverse roles, including seed oil synthesis, insect pheromone biosynthesis, and mammalian wax biosynthesis. In insects, FAR genes dedicated to sex pheromone biosynthesis (pheromone-gland-specific fatty acyl reductase, pgFAR) form a unique clade that exhibits substantial modifications in gene structure and possesses unique specificity and selectivity for fatty acyl substrates. Highly selective and semi-selective 'single pgFARs' produce single and multicomponent pheromone signals in bombycid, pyralid, yponomeutid and noctuid moths. An intriguing question is how a 'single reductase' can direct the synthesis of several fatty alcohols of various chain lengths and isomeric forms. Here, we report two active pgFARs in the pheromone gland of Spodoptera, namely a semi-selective, C14:acyl-specific pgFAR and a highly selective, C16:acyl-specific pgFAR, and demonstrate that these pgFARs play a pivotal role in the formation of species-specific signals, a finding that is strongly supported by functional gene expression data. The study envisages a new area of research for disclosing evolutionary changes associated with C<sub>14</sub> - and C<sub>16</sub> -specific FARs in moth pheromone biosynthesis.</p>},
  articleno    = {29927},
  author       = {Antony, Binu and Ding, Baojian and Moto, Ken'Ichi and Aldosari, Saleh A. and Aldawood, Abdulrahman S.},
  issn         = {2045-2322},
  language     = {eng},
  month        = {07},
  publisher    = {Nature Publishing Group},
  series       = {Scientific Reports},
  title        = {Two fatty acyl reductases involved in moth pheromone biosynthesis},
  url          = {http://dx.doi.org/10.1038/srep29927},
  volume       = {6},
  year         = {2016},
}