Identification of a diacylglycerol acyltransferase 2 gene involved in pheromone biosynthesis activating neuropeptide stimulated pheromone production in Bombyx mori

Du, Mingliang; Zhang, Songdou; Zhu, Bin; X, Yin; An, Shiheng

doi:10.1016/j.jinsphys.2012.02.002

Cited by 24 publications

(21 citation statements)

References 27 publications

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“…Our previous study identified a DGAT gene which regulates the biosynthesis of bombykol precursor, TAG9. The present study went further to demonstrate the role of GPAT, an upstream component of DGAT, in bombykol biosynthesis.…”

Section: Discussionmentioning

confidence: 52%

“…However TAG biosynthesis and storage are rarely investigated. Our previous study revealed that diacylglycerol acyltransferase 2 (DGAT) catalyses the final step in TAG biosynthesis, RNAi knockdown of DGAT causes a substantial decrease in sex pheromone production9. However TAG biosynthesis consists of two pathways, namely the monoacylglycerol (MAG) pathway and glycerol phosphate pathway (GAP).…”

Section: Discussionmentioning

confidence: 99%

“…A diacylglycerol acyltransferase 2 gene encoding for a speed-limiting enzyme of TAG biosynthesis was previously identified in B. mori PGs. RNAi knockdown of this gene significantly decreases bombykol production, suggesting that diacylglycerol acyltransferase 2 plays an important role in storage of TAGs, bombykol precursors9. After adult emergence, PBAN stimulates the lipolysis and subsequent reduction of LD TAGs to generate final bombykol10.…”

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confidence: 99%

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Glycerol-3-phosphate O-acyltransferase is required for PBAN-induced sex pheromone biosynthesis in Bombyx mori

Liu

et al. 2015

Sci Rep

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Female moths employ their own pheromone blends as a communicational medium in mating behavior. The biosynthesis and release of sex pheromone in female moths are regulated by pheromone biosynthesis activating neuropeptide (PBAN) and the corresponding action of PBAN has been well elucidated in Bombyx mori. However, very little is known about the molecular mechanism regarding the biosynthesis of sex pheromone precursor. In this study, quantitative proteomics was utilized to comprehensively elucidate the expression dynamics of pheromone glands (PGs) during development. Proteomic analysis revealed a serial of differentially expressed sex pheromone biosynthesis-associated proteins at the different time points of B. mori development. Most interestingly B. mori glycerol-3-phosphate O-acyltransferase (BmGPAT) was found to be expressed during the key periods of sex pheromone biosynthesis. RNAi knockdown of BmGPAT confirmed the important function of this protein in the biosynthesis of sex pheromone precursor, triacylglcerol (TAG), and subsequently PBAN-induced production of sex pheromone, bombykol. Behavioral analysis showed that RNAi knockdown of GPAT significantly impaired the ability of females to attract males. Our findings indicate that GPAT acts to regulate the biosynthesis of sex pheromone precursor, TAG, thus influencing PBAN-induced sex pheromone production and subsequent mating behavior.

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Section: Discussionmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Glycerol-3-phosphate O-acyltransferase is required for PBAN-induced sex pheromone biosynthesis in Bombyx mori

Liu

et al. 2015

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“…At that time the PG shows an increase in lipid droplets due to the accumulation of TG (Fonagy et al, 2001). In this regard, a recent study has shown that the expression of a “DGAT2” transcript in PG of Bombyx mori increases during the preparation for mating (Du et al, 2012). Our study suggests that the “BmDGAT2” gene actually encodes an MGAT-2 like protein.…”

Section: Discussionmentioning

confidence: 99%

Monoacylglycerol and diacylglycerol acyltransferases and the synthesis of neutral glycerides in Manduca sexta

Soulages

Firdaus

et al. 2015

Insect Biochemistry and Molecular Biology

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The insect fat body and the adipose tissue of vertebrates store fatty acids (FA) as triacylglycerols (TG). However, the fat body of most insects has the unique ability to rapidly produce and secrete large amounts of diacylglycerol (DG). Monoacylglycerol acyltransferase (MGAT), which catalyzes the synthesis of DG from MG, and a diacylglycerol acyltransferase (DGAT), which catalyzes the synthesis of TG from DG, are key enzymes in the metabolism of neutral glycerides. However, very little is known about these acyltransferases in insects. In the present study we have cloned two predicted MGATs and a DGAT from M. sexta and compared their sequences with predicted MGAT and DGAT homologues from a number of insect species. The comparison suggested that insects may only have a single DGAT gene, DGAT1. The apparent absence of a DGAT2 gene in insects would represent a major difference with vertebrates, which contain DGAT1 and DGAT2 genes. Insects seem to have a single MGAT gene which is similar to the MGAT2 of vertebrates. A number of conserved phosphorylation sites of potential physiological significance were identified among insect proteins and among insect and vertebrate proteins. DGAT1 and MGAT are expressed in fat body, midgut and ovaries. The relative rates of utilization of FAs for the synthesis of DG and TG correlated with the relative expression levels of MGAT and DGAT suggesting that regulation of the expression levels of these acyltransferases could be determining whether the fat body secretes DG or stores fatty acids as TG. The expression patterns of the acyltransferases suggest a role of the monoacylglycerol pathway in the production and mobilization of DG in M. sexta fat body.

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“…These include (i) acyltransferase involved in synthesis of FA-storing triacylglycerols [125,126]; (ii) lipases and esterases involved in hydrolytic release of FA pheromone precursors from storage triacylglycerols [127][128][129], formation of FA ethyl esters [130], or primary metabolism [131][132][133]; and (iii) cytochrome P450, involved in the oxidative decarbonylation of FAs to hydrocarbons [134]. However, for the majority of insect pheromone biosynthetic steps, the genes and enzymes involved have yet to be identified and characterized.…”

Section: Other Enzymesmentioning

confidence: 99%

Biotechnological potential of insect fatty acid-modifying enzymes

Tupec

Buček

Valterová

2017

Zeitschrift Für Naturforschung C

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There are more than one million described insect species. This species richness is reflected in the diversity of insect metabolic processes. In particular, biosynthesis of secondary metabolites, such as defensive compounds and chemical signals, encompasses an extraordinarily wide range of chemicals that are generally unparalleled among natural products from other organisms. Insect genomes, transcriptomes and proteomes thus offer a valuable resource for discovery of novel enzymes with potential for biotechnological applications. Here, we focus on fatty acid (FA) metabolism-related enzymes, notably the fatty acyl desaturases and fatty acyl reductases involved in the biosynthesis of FA-derived pheromones. Research on insect pheromone-biosynthetic enzymes, which exhibit diverse enzymatic properties, has the potential to broaden the understanding of enzyme specificity determinants and contribute to engineering of enzymes with desired properties for biotechnological production of FA derivatives. Additionally, the application of such pheromone-biosynthetic enzymes represents an environmentally friendly and economic alternative to the chemical synthesis of pheromones that are used in insect pest management strategies.

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Identification of a diacylglycerol acyltransferase 2 gene involved in pheromone biosynthesis activating neuropeptide stimulated pheromone production in Bombyx mori

Cited by 24 publications

References 27 publications

Glycerol-3-phosphate O-acyltransferase is required for PBAN-induced sex pheromone biosynthesis in Bombyx mori

Glycerol-3-phosphate O-acyltransferase is required for PBAN-induced sex pheromone biosynthesis in Bombyx mori

Monoacylglycerol and diacylglycerol acyltransferases and the synthesis of neutral glycerides in Manduca sexta

Biotechnological potential of insect fatty acid-modifying enzymes

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