PUBLICATION

Molecular cloning of a cold-shock domain protein, zfY1, in zebrafish embryo

Authors
Chang, B.E., Lin, C.Y., and Kuo, C.M.
ID
ZDB-PUB-990824-36
Date
1999
Source
BBA Protein Structure and Molecular Enzymology   1433(1-2): 343-349 (Journal)
Registered Authors
Chang, Bei-En
Keywords
cold-shock domain; Y box; zebrafish; rapid amplification of cDNA ends
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary/chemistry
  • DNA-Binding Proteins/chemistry
  • DNA-Binding Proteins/genetics*
  • Embryo, Nonmammalian/metabolism
  • Embryonic Development
  • Molecular Sequence Data
  • Phylogeny
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Zebrafish/embryology
  • Zebrafish/genetics*
PubMed
10446383 Full text @ BBA Protein Structure and Molecular Enzymology
Abstract
Cold-shock domain proteins in vertebrates contain a highly conserved domain which is related to the Escherichia coli cold-shock proteins. Here we report the cloning of a cold-shock domain protein from zebrafish embryo. Using the combination of PCR techniques with degenerate primers, 5'RACE and 3'RACE, the full length cDNA of a cold-shock domain protein in the zebrafish embryo was successfully cloned without constructing and screening a library. Determined from the deduced amino acid sequence, this protein is most similar to Xenopus, FRGY1, and this newly cloned zebrafish gene was therefore designated as zfY1.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping