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Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Functional diversification of teleost Fads2 fatty acyl desaturases occurs independently of the trophic level
Author(s): Garrido, Diego
Kabeya, Naoki
Betancor, Monica B
Perez, Jose A
Acosta, N Guadalupe
Tocher, Douglas R
Rodriguez, Covadonga
Monroig, Oscar
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Keywords: animal physiology
fatty acids
Issue Date: Aug-2019
Citation: Garrido D, Kabeya N, Betancor MB, Perez JA, Acosta NG, Tocher DR, Rodriguez C & Monroig O (2019) Functional diversification of teleost Fads2 fatty acyl desaturases occurs independently of the trophic level. Scientific Reports, 9, Art. No.: 11199.
Abstract: The long-chain (≥C20) polyunsaturated fatty acid biosynthesis capacity of fish varies among species, with trophic level hypothesised as a major factor. The biosynthesis capacity is largely dependent upon the presence of functionally diversified fatty acyl desaturase 2 (Fads2) enzymes, since many teleosts have lost the gene encoding a Δ5 desaturase (Fads1). The present study aimed to characterise Fads2 from four teleosts occupying different trophic levels, namely Sarpa salpa, Chelon labrosus, Pegusa lascaris and Atherina presbyter, which were selected based on available data on functions of Fads2 from closely related species. Therefore, we had insight into the variability of Fads2 within the same phylogenetic group. Our results showed that Fads2 from S. salpa and C. labrosus were both Δ6 desaturases with further Δ8 activity while P. lascaris and A. presbyter Fads2 showed Δ4 activity. Fads2 activities of herbivorous S. salpa are consistent with those reported for carnivorous Sparidae species. The results suggested that trophic level might not directly drive diversification of teleost Fads2 as initially hypothesised, and other factors such as the species’ phylogeny appeared to be more influential. In agreement, Fads2 activities from P. lascaris and A. presbyter were similar to their corresponding phylogenetic counterparts Solea senegalensis and Chirostoma estor.
DOI Link: 10.1038/s41598-019-47709-0
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