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Expression and characterization of nonmammalian selenoprotein P in the zebrafish, Danio rerio
Author(s) -
Tujebajeva Rosa M.,
Ransom David G.,
Harney John W.,
Berry Marla J.
Publication year - 2000
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2000.00375.x
Subject(s) - selenoprotein , zebrafish , biology , danio , selenocysteine , complementary dna , microbiology and biotechnology , selenoprotein p , gene , genetics , biochemistry , cysteine , enzyme , glutathione peroxidase , glutathione
Selenoprotein P is a protein of considerable intrigue, due to its unusual composition and requirements for its biosynthesis. Whereas most selenoproteins contain a single selenocysteine residue, the human, bovine and rodent selenoprotein P genes encode proteins containing 10–12 selenocysteines. Selenoprotein P genes have, to date, only been reported in mammals, and the function of the protein remains elusive. Herein, we report the identification and characterization of nonmammalian selenoprotein P in the zebrafish Danio rerio . Sequencing of the cDNA revealed the presence of 17 selenocysteine codons, the highest number reported in any protein. Two histidine‐rich regions present in the mammalian selenoprotein P sequences are conserved in the zebrafish protein, and two SECIS elements are present in the 3′ untranslated region. Whole‐mount in situ hybridization of zebrafish embryos revealed high levels of expression of selenoprotein P mRNA in fertilized eggs and in the yolk sac of developing embryos. Transient transfection of the cDNA in mammalian cells resulted in efficient expression of the full‐length secreted selenoprotein. A single N‐glycosylation site is predicted, and shown to be utilized. Discovery of selenoprotein P in the zebrafish opens a previously unavailable avenue for genetic investigation of the functions of this unusual protein.