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
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
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping