Birth-and-Death Evolution of the Fatty Acyl-CoA Reductase (FAR) Gene Family and Diversification of Cuticular Hydrocarbon Synthesis in Drosophila

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.

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Posttranslational Regulation of Fatty Acyl-CoA Reductase 1, Far1, Controls Ether Glycerophospholipid Synthesis

Journal of Biological Chemistry ◽

10.1074/jbc.m109.083311 ◽

2010 ◽

Vol 285 (12) ◽

pp. 8537-8542 ◽

Cited By ~ 69

Author(s):

Masanori Honsho ◽

Shunsuke Asaoku ◽

Yukio Fujiki

Keyword(s):

Fatty Acyl ◽

Posttranslational Regulation ◽

Coa Reductase

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Structural analysis of a hmg-coA-reductase pseudogene: insights into evolutionary processes affecting the hmgr gene family in allotetraploid cotton ( Gossypium hirsutum L.)

Current Genetics ◽

10.1007/s002940050393 ◽

1998 ◽

Vol 34 (4) ◽

pp. 241-249 ◽

Cited By ~ 15

Author(s):

L. L. Loguercio ◽

Thea A. Wilkins

Keyword(s):

Structural Analysis ◽

Gossypium Hirsutum ◽

Gene Family ◽

Evolutionary Processes ◽

Gossypium Hirsutum L ◽

Hmg Coa Reductase ◽

Coa Reductase ◽

Allotetraploid Cotton

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

10.1101/362509 ◽

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.

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Evolution of the codling moth pheromone via an ancient gene duplication

BMC Biology ◽

10.1186/s12915-021-01001-8 ◽

2021 ◽

Vol 19 (1) ◽

Author(s):

Jean-Marc Lassance ◽

Bao-Jian Ding ◽

Christer Löfstedt

Keyword(s):

Gene Family ◽

Developmental Stages ◽

Cydia Pomonella ◽

Fatty Acid Desaturase ◽

Codling Moth ◽

Fatty Acyl ◽

Integrative Approach ◽

Heterologous Expression Systems ◽

Genetic Novelty ◽

Ancient Gene

AbstractBackgroundDefining the origin of genetic novelty is central to our understanding of the evolution of novel traits. Diversification among fatty acid desaturase (FAD) genes has played a fundamental role in the introduction of structural variation in fatty acyl derivatives. Because of its central role in generating diversity in insect semiochemicals, the FAD gene family has become a model to study how gene family expansions can contribute to the evolution of lineage-specific innovations. Here we used the codling moth (Cydia pomonella) as a study system to decipher the proximate mechanism underlying the production of the ∆8∆10 signature structure of olethreutine moths. Biosynthesis of the codling moth sex pheromone, (E8,E10)-dodecadienol (codlemone), involves two consecutive desaturation steps, the first of which is unusual in that it generates anE9 unsaturation. The second step is also atypical: it generates a conjugated diene system from theE9 monoene C12intermediate via 1,4-desaturation.ResultsHere we describe the characterization of the FAD gene acting in codlemone biosynthesis. We identify 27 FAD genes corresponding to the various functional classes identified in insects and Lepidoptera. These genes are distributed across theC. pomonellagenome in tandem arrays or isolated genes, indicating that the FAD repertoire consists of both ancient and recent duplications and expansions. Using transcriptomics, we show large divergence in expression domains: some genes appear ubiquitously expressed across tissue and developmental stages; others appear more restricted in their expression pattern. Functional assays using heterologous expression systems reveal that one gene, Cpo_CPRQ, which is prominently and exclusively expressed in the female pheromone gland, encodes an FAD that possesses bothE9 and ∆8∆10 desaturation activities. Phylogenetically, Cpo_CPRQ clusters within the Lepidoptera-specific ∆10/∆11 clade of FADs, a classic reservoir of unusual desaturase activities in moths.ConclusionsOur integrative approach shows that the evolution of the signature pheromone structure of olethreutine moths relied on a gene belonging to an ancient gene expansion. Members of other expanded FAD subfamilies do not appear to play a role in chemical communication. This advises for caution when postulating the consequences of lineage-specific expansions based on genomics alone.

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Long-chain-fatty-acyl-CoA reductase

Enzyme Handbook ◽

10.1007/978-3-642-58051-2_45 ◽

1993 ◽

pp. 219-221

Author(s):

Dietmar Schomburg ◽

Margit Salzmann ◽

Dörte Stephan

Keyword(s):

Fatty Acyl ◽

Coa Reductase ◽

Long Chain

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Hepatic function in rats after spaceflight: effects on lipids, glycogen, and enzymes

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1987.252.2.r222 ◽

1987 ◽

Vol 252 (2) ◽

pp. R222-R226 ◽

Cited By ~ 3

Author(s):

A. H. Merrill ◽

E. Wang ◽

D. P. Jones ◽

J. L. Hargrove

Keyword(s):

Specific Activity ◽

Cytochrome B5 ◽

Hepatic Metabolism ◽

Microsomal Protein ◽

Hepatic Function ◽

Tyrosine Aminotransferase ◽

Fatty Acyl ◽

Blood Cholesterol ◽

Serine Palmitoyltransferase ◽

Coa Reductase

The inclusion of rats aboard Spacelab 3 (SL-3) allowed analyses of liver lipids, glycogen, hepatic enzymes of cholesterol, glycerolipid and sphingolipid biosynthesis, and other enzyme activities. Glycogen content was markedly elevated in livers from the flight animals compared with controls. Cholesterol was 24% (P less than 0.04) lower in livers from the experimental groups, whereas blood cholesterol was 19% higher (P less than 0.05). The activity of 3-hydroxy-3-methylglutaryl-CoA reductase, the rate-limiting enzyme of steroid biosynthesis, was 80% lower (P less than 0.01). Total phospholipids and sphingolipid levels did not differ significantly. The specific activity of fatty acyl-CoA synthetase, which is responsible for activation of fatty acids, was 37% (P less than 0.05) higher in microsomes from the rats on SL-3; however, since these animals had 25% less microsomal protein (P less than 0.02), there was no difference per gram of liver. The initial enzymes of sphingolipid and glycerolipid biosynthesis were assayed; serine palmitoyltransferase was 40% lower (P less than 0.01), and glycerol 3-phosphate acyltransferase did not differ. Hepatic cytochrome P-450 content decreased by 50% after spaceflight. Enzymes that did not differ significantly between the two groups include cytochrome b5, glutathione S-transferase, tyrosine aminotransferase, aspartate aminotransferase, and cystathionase. These findings suggest that spaceflight alters hepatic metabolism of several classes of compounds.

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