FN Archimer Export Format
PT J
TI Cloning, Tissue Expression Analysis, and Functional Characterization of Two Δ6-Desaturase Variants of Sea Bass (Dicentrarchus labrax L.)
BT 
AF SANTIGOSA, Ester
   GEAY, Florian
   TONON, Thierry
   LE DELLIOU, Herve
   KUHL, Heiner
   REINHARDT, Richard
   CORCOS, Laurent
   CAHU, Chantal
   ZAMBONINO-INFANTE, Jose-Luis
   MAZURAIS, David
AS 1:1;2:1;3:2,3;4:1;5:4;6:4;7:5,6;8:1;9:1;10:1;
FF 1:;2:PDG-RBE-PFOM-ARN;3:;4:PDG-RBE-PFOM-ARN;5:;6:;7:;8:PDG-RBE-PFOM;9:PDG-RBE-PFOM-ARN;10:PDG-RBE-PFOM-ARN;
C1 IFREMER, Ifremer Marine Fish Nutr Team, Nutr Aquaculture & Genom Res Unit, UMR 1067, F-29280 Plouzane, France.
   Univ Paris 06, UMR Vegetaux Marins & Biomol 7139, Biol Stn, F-29682 Roscoff, France.
   CNRS, UMR Vegetaux Marins & Biomol 7139, Biol Stn, F-29682 Roscoff, France.
   Max Planck Inst Mol Genet, D-14195 Berlin, Germany.
   Univ Brest, INSERM, U613, ECLA, F-29200 Brest, France.
   Univ Europeenne Bretagne, Fac Med, F-29200 Brest, France.
C2 IFREMER, FRANCE
   UNIV PARIS 06, FRANCE
   CNRS, FRANCE
   INST MAX PLANCK (MOL GENET), GERMANY
   UBO, FRANCE
   UEB, FRANCE
SI BREST
SE PDG-RBE-PFOM-ARN
   PDG-RBE-PFOM
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-europe
   copubli-univ-france
IF 3.43
TC 29
UR https://archimer.ifremer.fr/doc/00023/13470/10477.pdf
LA English
DT Article
DE ;Sea bass (Dicentrarchus labrax);Desaturase;HUFA biosynthesis;Fish;EPA
AB Fish are the main source of the n-3 highly unsaturated fatty acids, which are crucial for human health. Their synthesis from C18 precursors is mediated by desaturases and elongases, but the activity of these enzymes has not been conclusively established in marine fish species. This study reports the cloning, tissue expression, and functional characterization of a sea bass (Dicentrarchus labrax L.) Δ6-desaturase and one of its splicing variants. Two cDNAs with open reading frames of 1,346 and 1,354 bp were cloned and named D6D and D6D-V, respectively. Both deduced protein sequences (445 and 387 amino acids, respectively) contained two transmembrane regions and the N-terminal cytochrome b5 domain with the HPGG motif characteristic of microsomal desaturases. D6D presents three histidine-rich regions, whereas in D6D-V, an insertion of eight nucleotides in the boundaries of exons 10 and 11 modified the third histidine-rich domain and led to insertion of a premature STOP codon, resulting in a shorter predicted protein. Quantitative real-time polymerase chain reaction assay of gene expression showed that D6D was highly expressed in the brain and intestine, and to a lesser extent, in muscle and liver; meanwhile, D6D-V was expressed in all tissues tested, but at level at least 200-fold lower than D6D. Functional analysis in yeast showed that sea bass D6D encodes a fully functional Δ6-desaturase with no residual Δ5-desaturase activity. This desaturase does not exhibit a clear preference for n-3 versus n-6 C18 substrates. Interestingly, D6D-V is a nonfunctional protein, suggesting that the C-terminal end is indispensable for protein activity.
PY 2011
PD FEB
SO Marine Biotechnology
SN 1436-2228
PU Springer
VL 13
IS 1
UT 000288022600003
BP 22
EP 31
DI 10.1007/s10126-010-9264-4
ID 13470
ER

EF