Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor.

Autor:	Fonseca-Madrigal J; Laboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico., Navarro JC; Instituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain., Hontoria F; Instituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain., Tocher DR; Institute of Aquaculture, School of Natural Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK., Martínez-Palacios CA; Laboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico., Monroig Ó; Instituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain Laboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico.
Jazyk:	angličtina
Zdroj:	Journal of lipid research [J Lipid Res] 2014 Jul; Vol. 55 (7), pp. 1408-19. Date of Electronic Publication: 2014 May 02.
DOI:	10.1194/jlr.M049791
Abstrakt:	Currently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fish is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during evolution. We previously showed that Chirostoma estor, one of the few representatives of freshwater atherinopsids, had the ability for LC-PUFA biosynthesis from C18 PUFA precursors, in agreement with this species having unusually high contents of DHA. The particular ancestry and pattern of LC-PUFA biosynthesis activity of C. estor make this species an excellent model for study to gain further insight into LC-PUFA biosynthetic abilities among teleosts. The present study aimed to characterize cDNA sequences encoding fatty acyl elongases and desaturases, key genes involved in the LC-PUFA biosynthesis. Results show that C. estor expresses an elongase of very long-chain FA (Elovl)5 elongase and two Fads2 desaturases displaying Δ4 and Δ6/Δ5 specificities, thus allowing us to conclude that these three genes cover all the enzymatic abilities required for LC-PUFA biosynthesis from C18 PUFA. In addition, the specificities of the C. estor Fads2 enabled us to propose potential evolutionary patterns and mechanisms for subfunctionalization of Fads2 among fish lineages. (Copyright © 2014 by the American Society for Biochemistry and Molecular Biology, Inc.)
Databáze:	MEDLINE
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