scholarly journals Expansion of the fatty acyl reductase gene family shaped pheromone communication in Hymenoptera

2018 ◽  
Author(s):  
Michal Tupec ◽  
Aleš Buček ◽  
Heiko Vogel ◽  
Václav Janoušek ◽  
Darina Prchalová ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Gene Family ◽  
Fat Body ◽  
Functional Characterization ◽  
Acid Methyl Ester ◽  
Fatty Acyl ◽  
Sequencing Analysis ◽  
Pheromone Communication ◽  
Marking Pheromone ◽  
Fatty Acyl Reductase

AbstractThe conserved fatty acyl reductase (FAR) family is involved in biosynthesis of fatty alcohols that serve a range of biological roles. In moths, butterflies (Lepidoptera), and bees (Hymenoptera), FARs biosynthesize fatty alcohol pheromones participating in mate-finding strategies. Using a combination of next-generation sequencing, analysis of transposable elements (TE) in the genomic environment of FAR genes, and functional characterization of FARs from Bombus lucorum, B. lapidarius, and B. terrestris, we uncovered a massive expansion of the FAR gene family in Hymenoptera, presumably facilitated by TEs. Expansion occurred in the common ancestor of bumblebees (Bombini) and stingless bees (Meliponini) after their divergence from the honeybee lineage. We found that FARs from the expanded FAR-A orthology group contributed to the species-specific male marking pheromone composition. Our results indicate that TE-mediated expansion and functional diversification of the FAR gene family played a key role in the evolution of pheromone communication in the crown group of Hymenoptera.AbbreviationsMMP: male marking pheromone, FA: fatty acid, FAME: fatty acid methyl ester, FAR: fatty acyl reductase, LG: labial gland, FB: fat body, TE: transposable element.

scholarly journals Expansion of the fatty acyl reductase gene family shaped pheromone communication in Hymenoptera

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Michal Tupec ◽  
Aleš Buček ◽  
Václav Janoušek ◽  
Heiko Vogel ◽  
Darina Prchalová ◽  
...  
Keyword(s):  
Gene Family ◽  
Functional Characterization ◽  
Gene Tree ◽  
Biological Significance ◽  
Fatty Acyl ◽  
Pheromone Biosynthesis ◽  
Bumble Bee ◽  
Pheromone Communication ◽  
Genomic Environment ◽  
Species Specific

Fatty acyl reductases (FARs) are involved in the biosynthesis of fatty alcohols that serve a range of biological roles. Insects typically harbor numerous FAR gene family members. While some FARs are involved in pheromone biosynthesis, the biological significance of the large number of FARs in insect genomes remains unclear.Using bumble bee (Bombini) FAR expression analysis and functional characterization, hymenopteran FAR gene tree reconstruction, and inspection of transposable elements (TEs) in the genomic environment of FARs, we uncovered a massive expansion of the FAR gene family in Hymenoptera, presumably facilitated by TEs. The expansion occurred in the common ancestor of bumble bees and stingless bees (Meliponini). We found that bumble bee FARs from the expanded FAR-A ortholog group contribute to the species-specific pheromone composition. Our results indicate that expansion and functional diversification of the FAR gene family played a key role in the evolution of pheromone communication in Hymenoptera.

scholarly journals Author response: Expansion of the fatty acyl reductase gene family shaped pheromone communication in Hymenoptera

2018 ◽  
Author(s):  
Michal Tupec ◽  
Aleš Buček ◽  
Václav Janoušek ◽  
Heiko Vogel ◽  
Darina Prchalová ◽  
...  
Keyword(s):  
Gene Family ◽  
Fatty Acyl ◽  
Author Response ◽  
Pheromone Communication ◽  
Reductase Gene ◽  
Fatty Acyl Reductase

scholarly journals Functional Characterization of Desaturases Involved in the Formation of the Terminal Double Bond of an Unusual 16:3Δ9, 12, 15 Fatty Acid Isolated from Sorghum bicolor Root Hairs

2006 ◽  
Vol 282 (7) ◽  
pp. 4326-4335 ◽  
Author(s):  
Zhiqiang Pan ◽  
Agnes M. Rimando ◽  
Scott R. Baerson ◽  
Mark Fishbein ◽  
Stephen O. Duke
Keyword(s):  
Fatty Acid ◽  
Double Bond ◽  
Sorghum Bicolor ◽  
Expressed Sequence Tag ◽  
Functional Characterization ◽  
Root Hairs ◽  
Fatty Acyl ◽  
Aliphatic Chain ◽  
Fatty Acid Desaturases ◽  
Terminal Double Bond

Sorgoleone, produced in root hair cells of sorghum (Sorghum bicolor), is likely responsible for much of the allelopathic properties of sorghum root exudates against broadleaf and grass weeds. Previous studies suggest that the biosynthetic pathway of this compound initiates with the synthesis of an unusual 16:3 fatty acid possessing a terminal double bond. The corresponding fatty acyl-CoA serves as a starter unit for polyketide synthases, resulting in the formation of 5-pentadecatrienyl resorcinol. This resorcinolic intermediate is then methylated by an S-adenosylmethionine-dependent O-methyltransferase and subsequently dihydroxylated, yielding the reduced (hydroquinone) form of sorgoleone. To characterize the corresponding enzymes responsible for the biosynthesis of the 16:3 fatty acyl-CoA precursor, we identified and cloned three putative fatty acid desaturases, designated SbDES1, SbDES2, and SbDES3, from an expressed sequence tag (EST) data base prepared from isolated root hairs. Quantitative real-time RT-PCR analyses revealed that these three genes were preferentially expressed in sorghum root hairs where the 16:2 and 16:3 fatty acids were exclusively localized. Heterologous expression of the cDNAs in Saccharomyces cerevisiae revealed that recombinant SbDES2 converted palmitoleic acid (16:1Δ9) to hexadecadienoic acid (16:2Δ9,12), and that recombinant SbDES3 was capable of converting hexadecadienoic acid into hexadecatrienoic acid (16:3Δ9,12,15). Unlike other desaturases reported to date, the double bond introduced by SbDES3 occurred between carbons 15 and 16 resulting in a terminal double bond aliphatic chain. Collectively, the present results strongly suggest that these fatty acid desaturases represent key enzymes involved in the biosynthesis of the allelochemical sorgoleone.

scholarly journals Birth-and-death evolution of the fatty acyl-CoA reductase (FAR) gene family and diversification of cuticular hydrocarbon synthesis in Drosophila

2019 ◽  
Author(s):  
Cédric Finet ◽  
Kailey Slavik ◽  
Jian Pu ◽  
Sean B. Carroll ◽  
Henry Chung
Keyword(s):  
Fatty Acid ◽  
Gene Family ◽  
Cuticular Hydrocarbon ◽  
Evolutionary Model ◽  
Gene Families ◽  
Single Copy ◽  
Fatty Acyl ◽  
Comparative Approach ◽  
Hydrocarbon Synthesis ◽  
Functional Studies

AbstractThe birth-and-death evolutionary model proposes that some members of a multigene family are phylogenetically stable and persist as a single copy over time whereas other members are phylogenetically unstable and undergo frequent duplication and loss. Functional studies suggest that stable genes are likely to encode essential functions, while rapidly evolving genes reflect phenotypic differences in traits that diverge rapidly among species. One such class of rapidly diverging traits are insect cuticular hydrocarbons (CHCs), which play dual roles in chemical communications as short-range recognition pheromones as well as protecting the insect from desiccation. Insect CHCs diverge rapidly between related species leading to ecological adaptation and/or reproductive isolation. Because the CHC and essential fatty acid biosynthetic pathways share common genes, we hypothesized that genes involved in the synthesis of CHCs would be evolutionary unstable, while those involved in fatty acid-associated essential functions would be evolutionary stable. To test this hypothesis, we investigated the evolutionary history of the fatty acyl-CoA reductases (FARs) gene family that encodes enzymes in CHC synthesis. We compiled a unique dataset of 200 FAR proteins across 12 Drosophila species. We uncovered a broad diversity in FAR content which is generated by gene duplications, subsequent gene losses, and alternative splicing. We also show that FARs expressed in oenocytes and presumably involved in CHC synthesis are more unstable than FARs from other tissues. We suggest that a comparative approach investigating the birth-and-death evolution of gene families can identify candidate genes involved in rapidly diverging traits between species.

scholarly journals Evolution of moth sex pheromone composition by a single amino acid substitution in a fatty acid desaturase

2015 ◽  
Vol 112 (41) ◽  
pp. 12586-12591 ◽  
Author(s):  
Aleš Buček ◽  
Petra Matoušková ◽  
Heiko Vogel ◽  
Petr Šebesta ◽  
Ullrich Jahn ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Substitution ◽  
Functional Characterization ◽  
Fatty Acid Desaturase ◽  
Fatty Acyl ◽  
Site Directed Mutagenesis ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

For sexual communication, moths primarily use blends of fatty acid derivatives containing one or more double bonds in various positions and configurations, called sex pheromones (SPs). To study the molecular basis of novel SP component (SPC) acquisition, we used the tobacco hornworm (Manduca sexta), which uses a blend of mono-, di-, and uncommon triunsaturated fatty acid (3UFA) derivatives as SP. We identified pheromone-biosynthetic fatty acid desaturases (FADs) MsexD3, MsexD5, and MsexD6 abundantly expressed in the M. sexta female pheromone gland. Their functional characterization and in vivo application of FAD substrates indicated that MsexD3 and MsexD5 biosynthesize 3UFAs via E/Z14 desaturation from diunsaturated fatty acids produced by previously characterized Z11-desaturase/conjugase MsexD2. Site-directed mutagenesis of sequentially highly similar MsexD3 and MsexD2 demonstrated that swapping of a single amino acid in the fatty acyl substrate binding tunnel introduces E/Z14-desaturase specificity to mutated MsexD2. Reconstruction of FAD gene phylogeny indicates that MsexD3 was recruited for biosynthesis of 3UFA SPCs in M. sexta lineage via gene duplication and neofunctionalization, whereas MsexD5 representing an alternative 3UFA-producing FAD has been acquired via activation of a presumably inactive ancestral MsexD5. Our results demonstrate that a change as small as a single amino acid substitution in a FAD enzyme might result in the acquisition of new SP compounds.

scholarly journals Cryptosporidium parvum Long-Chain Fatty Acid Elongase

2007 ◽  
Vol 6 (11) ◽  
pp. 2018-2028 ◽  
Author(s):  
Jason M. Fritzler ◽  
Jason J. Millership ◽  
Guan Zhu
Keyword(s):  
Fatty Acid ◽  
Functional Characterization ◽  
Fatty Acyl ◽  
Chain Fatty Acid ◽  
Type I ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Elongase ◽  
Key Enzyme ◽  
Acyl Coenzyme A ◽  
Long Chain

ABSTRACT We report the presence of a new fatty acyl coenzyme A (acyl-CoA) elongation system in Cryptosporidium and the functional characterization of the key enzyme, a single long-chain fatty acid elongase (LCE), in this parasite. This enzyme contains conserved motifs and predicted transmembrane domains characteristic to the elongase family and is placed within the ELO6 family specific for saturated substrates. CpLCE1 gene transcripts are present at all life cycle stages, but the levels are highest in free sporozoites and in stages at 36 h and 60 h postinfection that typically contain free merozoites. Immunostaining revealed localization to the outer surface of sporozoites and to the parasitophorous vacuolar membrane. Recombinant CpLCE1 displayed allosteric kinetics towards malonyl-CoA and palmitoyl-CoA and Michaelis-Menten kinetics towards NADPH. Myristoyl-CoA (C14:0) and palmitoyl-CoA (C16:0) display the highest activity when used as substrates, and only one round of elongation occurs. CpLCE1 is fairly resistant to cerulenin, an inhibitor for both type I and II fatty acid synthases (i.e., maximum inhibitions of 20.5% and 32.7% were observed when C16:0 and C14:0 were used as substrates, respectively). These observations ultimately validate the function of CpLCE1.

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