PUBLICATION
Zebrafish translation elongation factor EF1 alpha mRNA: sequence and secondary structures
- Authors
- Gao, D., Dalton, M., Li, Z., Murphy, T., Kitzan, M., Sauerbier, A., and Sauerbier, W.
- ID
- ZDB-PUB-970324-9
- Date
- 1996
- Source
- Molecular marine biology and biotechnology 5(4): 288-294 (Journal)
- Registered Authors
- Li, Zheng, Sauerbier, W.
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Composition
- Base Sequence
- Biological Evolution
- Cloning, Molecular
- DNA, Complementary/genetics
- Flatfishes/embryology
- Flatfishes/genetics
- Molecular Sequence Data
- Nucleic Acid Conformation*
- Peptide Elongation Factor 1
- Peptide Elongation Factors/genetics*
- RNA, Messenger/genetics*
- Ribosomal Proteins/genetics
- Sequence Analysis, DNA
- Sequence Homology, Nucleic Acid
- Species Specificity
- Zebrafish/embryology
- Zebrafish/genetics*
- PubMed
- 8983197
Citation
Gao, D., Dalton, M., Li, Z., Murphy, T., Kitzan, M., Sauerbier, A., and Sauerbier, W. (1996) Zebrafish translation elongation factor EF1 alpha mRNA: sequence and secondary structures. Molecular marine biology and biotechnology. 5(4):288-294.
Abstract
We have determined the complete sequence of the translation elongation factor EF1 subunit alpha (EF1 alpha) mRNA of zebrafish, and the 3'-untranslated sequence of EF1 alpha mRNA of halibut. The 5'-untranslated leader sequence of the EF1 alpha mRNA starts with a polypyrimidine tract. This feature is shared with the mRNAs for ribosomal proteins, where it affects the utilization of mRNA by ribosomes. However, the secondary structures of these leader sequences may differ. 5'- Polypyrimidine tracts of vertebrate EF1 alpha mRNAs participate in the formation of stable stem-loop structures, whereas those of 15 randomly chosen mRNAs for ribosomal proteins do not. This difference may provide a basis for differential control of translation for the two classes of mRNA. The 3'-untranslated sequences of vertebrate EF1 alpha mRNA have diverged little during evolution. Analyses of sequence and putative secondary structures suggest that both sequence-specific interactions and secondary structures may have contributed to sequence conservation.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping