Identification and characterization of a fatty acyl reductase from aSpodoptera littoralisfemale gland involved in pheromone biosynthesis

2014 ◽  
Vol 24 (1) ◽  
pp. 82-92 ◽  
Author(s):  
G. Carot-Sans ◽  
L. Muñoz ◽  
M. D. Piulachs ◽  
A. Guerrero ◽  
G. Rosell
Keyword(s):  
Fatty Acyl ◽  
Pheromone Biosynthesis ◽  
Fatty Acyl Reductase ◽  
Identification And Characterization

scholarly journals Transcriptome Analysis of Ostrinia furnacalis Female Pheromone Gland: Esters Biosynthesis and Requirement for Mating Success

2021 ◽  
Vol 12 ◽  
Author(s):  
Shuangyan Yao ◽  
Shuai Zhou ◽  
Xiang Li ◽  
Xiaoguang Liu ◽  
Wenli Zhao ◽  
...  
Keyword(s):  
Sex Pheromone ◽  
Candidate Genes ◽  
Model Organism ◽  
Fatty Acyl ◽  
Pheromone Biosynthesis ◽  
Mrna Levels ◽  
Ostrinia Furnacalis ◽  
Sex Pheromone Biosynthesis ◽  
Secondary Messenger ◽  
Fatty Acyl Reductase

Female moths use sex pheromones to attract males, and corresponding regulatory mechanism underlying sex pheromone biosynthesis is species-dependent. However, the detailed mechanism involved in sex pheromone biosynthesis in Ostrinia furnacalis has not yet been fully addressed. In the present study, transcriptome sequencing of O. furnacalis pheromone glands screened a serials of candidate genes involved in sex pheromone biosynthesis. Our analysis showed that sex pheromone release in O. furnacalis females arrives its peak at the 2nd scotophase, consistent with its mating behavior. Pheromone biosynthesis-activating neuropeptide (PBAN) was confirmed to regulate sex pheromone biosynthesis, and Ca2+ is the secondary messenger of PBAN signaling in O. furnacalis. The functional analysis of candidate genes demonstrated that the decreased mRNA levels or activities of calcineurin (CaN) and acetyl-CoA carboxylase (ACC) led to significant decrease in sex pheromone production and female capability to attract males, as demonstrated by RNAi-mediated knockdown and pharmacological inhibitor assay. Most importantly, the activities of CaN and ACC depend on the activation of PBAN/PBANR/Ca2+. Furthermore, fatty-acyl reductase 14 was involved in PBAN-mediated sex pheromone biosynthesis. Altogether, our results demonstrated that PBAN regulates sex pheromone biosynthesis through PBANR/Ca2+/CaN/ACC pathway to promote sex pheromone biosynthesis in O. furnacalis and provided a reference for non-model organism to study neuropeptide signal transduction.

scholarly journals Identification and Characterization of the Genes Involved in Glycosylation Pathways of Mycobacterial Glycopeptidolipid Biosynthesis

2006 ◽  
Vol 188 (1) ◽  
pp. 86-95 ◽  
Author(s):  
Yuji Miyamoto ◽  
Tetsu Mukai ◽  
Noboru Nakata ◽  
Yumi Maeda ◽  
Masanori Kai ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acyl ◽  
Gas Chromatography Mass Spectrometry ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
The Common ◽  
Glycosylation Pathway ◽  
Layer Chromatography ◽  
Identification And Characterization

ABSTRACT Glycopeptidolipids (GPLs) are major components present on the outer layers of the cell walls of several nontuberculous mycobacteria. GPLs are antigenic molecules and have variant oligosaccharides in mycobacteria such as Mycobacterium avium. In this study, we identified four genes (gtf1, gtf2, gtf3, and gtf4) in the genome of Mycobacterium smegmatis. These genes were independently inactivated by homologous recombination in M. smegmatis, and the structures of GPLs from each gene disruptant were analyzed. Thin-layer chromatography, gas chromatography-mass spectrometry, and matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analyses revealed that the mutants Δgtf1 and Δgtf2 accumulated the fatty acyl-tetrapeptide core having O-methyl-rhamnose and 6-deoxy-talose as sugar residues, respectively. The mutant Δgtf4 possessed the same GPLs as the wild type, whereas the mutant Δgtf3 lacked two minor GPLs, consisting of 3-O-methyl-rhamnose attached to O-methyl-rhamnose of the fatty acyl-tetrapeptide core. These results indicate that the gtf1 and gtf2 genes are responsible for the early glycosylation steps of GPL biosynthesis and the gtf3 gene is involved in transferring a rhamnose residue not to 6-deoxy-talose but to an O-methyl-rhamnose residue. Moreover, a complementation experiment showed that M. avium gtfA and gtfB, which are deduced glycosyltransferase genes of GPL biosynthesis, restore complete GPL production in the mutants Δgtf1 and Δgtf2, respectively. Our findings propose that both M. smegmatis and M. avium have the common glycosylation pathway in the early steps of GPL biosynthesis but differ at the later stages.

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