PUBLICATION
Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues
- Authors
- Kryukov, G.V. and Gladyshev, V.N.
- ID
- ZDB-PUB-010219-12
- Date
- 2000
- Source
- Genes to cells : devoted to molecular & cellular mechanisms 5(12): 1049-1060 (Journal)
- Registered Authors
- Gladyshev, Vadim, Kryukov, Gregory
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Cell Line
- Chlorocebus aethiops
- DNA, Complementary/chemistry
- Gene Duplication
- Humans
- Molecular Sequence Data
- Multigene Family*
- Phylogeny
- Protein Biosynthesis*
- Proteins/genetics*
- Proteins/isolation & purification
- Proteins/metabolism
- Selenium/metabolism*
- Selenocysteine/metabolism*
- Selenoprotein P
- Selenoprotein W
- Selenoproteins
- Sequence Alignment
- Sequence Homology, Amino Acid
- Zebrafish
- Zebrafish Proteins
- PubMed
- 11168591 Full text @ Genes Cells
Citation
Kryukov, G.V. and Gladyshev, V.N. (2000) Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues. Genes to cells : devoted to molecular & cellular mechanisms. 5(12):1049-1060.
Abstract
Fish are an important source of selenium in human nutrition and the zebrafish is a potentially useful model organism for the study of selenium metabolism and its role in biology and medicine. Selenium is present in vertebrate proteins in the form of selenocysteine (Sec), the 21st natural amino acid in protein which is encoded by UGA. We report here the detection of 18 zebrafish genes for Sec-containing proteins. We found two zebrafish orthologs of human SelT, glutathione peroxidase 1 and glutathione peroxidase 4, and single orthologs of several other selenoproteins. In addition, new zebrafish selenoproteins were identified that were distant homologues of SelP, SelT and SelW, but their direct orthologs in other species are not known. This multiplicity of selenoprotein genes appeared to result from gene and genome duplications, followed by the retention of new selenoprotein genes. We found a zebrafish selenoprotein P gene (designated zSelPa) that contained two Sec insertion sequence (SECIS) elements and encoded a protein containing 17 Sec residues, the largest number of Sec residues found in any known protein. In contrast, a second SelP gene (designated zSelPb) was also identified that contained one SECIS element and encoded a protein with a single Sec. We found that zSelPa could be expressed and secreted by mammalian cells. The occurrence of zSelPa and zSelPb suggested that the function of the N-terminal domain of mammalian SelP proteins may be separated from that of the C-terminal Sec-rich sequence: the N-terminal domain containing the UxxC motif is likely involved in oxidoreduction, whereas the C-terminal portion of the protein may function in selenium transport or storage. Our data also suggest that the utilization of Sec is more common in zebrafish than in previously characterized species, including mammals.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping