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Functional identification of fatty acyl reductases in female pheromone gland and tarsi of the corn earworm, Helicoverpa zea.

Authors :
Dou X
Zhang A
Jurenka R
Source :
Insect biochemistry and molecular biology [Insect Biochem Mol Biol] 2020 Jan; Vol. 116, pp. 103260. Date of Electronic Publication: 2019 Nov 01.
Publication Year :
2020

Abstract

Most moths utilize sex pheromones released by the female to attract a mate. Females produce the sex pheromone in the pheromone gland in a biosynthetic pathway which consists of several key enzymes. Fatty acyl-CoA reductase is one of the key enzymes, which catalyzes the conversion of fatty acyl-CoA to the corresponding alcohol, playing an important role in producing the final proportion of each pheromone component. In Helicoverpa zea, (Z)-11-hexadecenal is the major sex pheromone component in female pheromone glands and previously a large amount of hexadecanal was also found in female and male tarsi. In our previous study, we compared the transcriptome between pheromone glands and tarsi and found 20 fatty acyl-CoA reductases in both tissues. In this study, we functionally characterized four FARs which were expressed at high levels according to the transcriptome of pheromone glands and tarsi. Fatty acyl-CoA reductase 1 was homologous to other moth pheromone gland specific fatty acyl-CoA reductases, and it was also present in male tarsi. Functional expression in yeast cells indicates that only fatty acyl-CoA reductase 1 was able to produce fatty alcohols. In addition, a decreased mRNA level of fatty acyl-CoA reductase 1 in female pheromone glands and male tarsi by RNAi knockdown caused a significant decrease in the production of (Z)-11-hexadecenal in pheromone glands and hexadecanal in male tarsi. This study is the first to demonstrate the direct function of a fatty acyl-CoA reductase in male tarsi and also confirms its role in sex pheromone biosynthesis in H. zea.<br /> (Copyright © 2019 Elsevier Ltd. All rights reserved.)

Details

Language :
English
ISSN :
1879-0240
Volume :
116
Database :
MEDLINE
Journal :
Insect biochemistry and molecular biology
Publication Type :
Academic Journal
Accession number :
31682920
Full Text :
https://doi.org/10.1016/j.ibmb.2019.103260