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