PUBLICATION
Expression and characterization of nonmammalian selenoprotein P in the zebrafish, Danio rerio
- Authors
- Tujebajeva, R.M., Ransom, D.G., Harney, J.W., and Berry, M.J.
- ID
- ZDB-PUB-001221-1
- Date
- 2000
- Source
- Genes to cells : devoted to molecular & cellular mechanisms 5(11): 897-903 (Journal)
- Registered Authors
- Ransom, David G.
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence/genetics
- Animals
- Cell Line
- Gene Expression
- Glycosylation
- Humans
- In Situ Hybridization
- Molecular Sequence Data
- Organ Specificity
- Physical Chromosome Mapping
- Protein Biosynthesis*
- Proteins/chemistry
- Proteins/genetics*
- RNA, Messenger/biosynthesis
- Selenium Radioisotopes
- Selenoprotein P
- Selenoproteins
- Sequence Analysis, DNA
- Sequence Homology, Amino Acid
- Transfection
- Zebrafish
- Zebrafish Proteins
- PubMed
- 11122377 Full text @ Genes Cells
Citation
Tujebajeva, R.M., Ransom, D.G., Harney, J.W., and Berry, M.J. (2000) Expression and characterization of nonmammalian selenoprotein P in the zebrafish, Danio rerio. Genes to cells : devoted to molecular & cellular mechanisms. 5(11):897-903.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping