title: Two fatty acyl reductases involved in moth pheromone biosynthesis.
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 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.
authors.affiliation: King Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
authors.forename: Binu
authors.initials: B
authors.lastname: Antony
authors.affiliation: Lund University, Department of Biology, Lund 22362, Sweden.
authors.forename: Bao-Jian
authors.initials: BJ
authors.lastname: Ding
authors.affiliation: RIKEN, Lipid Biology Laboratory, Wako, Saitama 351-0198, Japan.
authors.forename: Ken'Ichi
authors.initials: K
authors.lastname: Moto
authors.affiliation: King Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
authors.forename: Saleh A
authors.initials: SA
authors.lastname: Aldosari
authors.affiliation: King Saud University, Department of Plant Protection, Chair of Date Palm Research, College of Food and Agricultural Sciences, Riyadh 11451, Saudi Arabia.
authors.forename: Abdulrahman S
authors.initials: AS
authors.lastname: Aldawood
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000825:Animal Structures / Q000378:metabolism; D000818:Animals; D001681:Biological Assay; D053898:Biosynthetic Pathways; D003001:Cloning, Molecular; D005227:Fatty Acids / Q000378:metabolism; D005233:Fatty Alcohols / Q000378:metabolism; D008401:Gas Chromatography-Mass Spectrometry; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism*; D016013:Likelihood Functions; D009036:Moths / Q000201:enzymology*; D009928:Organ Specificity; D010802:Phylogeny; D060888:Real-Time Polymerase Chain Reaction; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D012724:Sex Attractants / Q000096:biosynthesis*; D013379:Substrate Specificity
chemical_list: D005227:Fatty Acids; D005233:Fatty Alcohols; D019476:Insect Proteins; D012724:Sex Attractants; D000445:Aldehyde Oxidoreductases