PUBLICATION
Two zebrafish eIF4E family members are differentially expressed and functionally divergent
- Authors
- Robalino, J., Joshi, B., Fahrenkrug, S.C., and Jagus, R.
- ID
- ZDB-PUB-040109-18
- Date
- 2004
- Source
- The Journal of biological chemistry 279(11): 10532-10541 (Journal)
- Registered Authors
- Fahrenkrug, Scott C., Jagus, Rosemary
- Keywords
- none
- MeSH Terms
-
- Adaptor Proteins, Signal Transducing
- Amino Acid Sequence
- Animals
- Biological Evolution
- Carrier Proteins/metabolism
- DNA, Complementary/metabolism
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli/metabolism
- Eukaryotic Initiation Factor-4E/biosynthesis*
- Eukaryotic Initiation Factor-4E/physiology*
- Eukaryotic Initiation Factors/metabolism
- Female
- Genetic Complementation Test
- Genetic Vectors
- Glutathione Transferase/metabolism
- Humans
- Immunoblotting
- Isoelectric Focusing
- Male
- Molecular Sequence Data
- Multigene Family
- Ovary/metabolism
- Phosphoproteins/metabolism
- Plasmids/metabolism
- Protein Binding
- Protein Biosynthesis
- Protein Structure, Tertiary
- RNA, Messenger/metabolism
- Recombinant Proteins/chemistry
- Reverse Transcriptase Polymerase Chain Reaction
- Saccharomyces cerevisiae/metabolism
- Sequence Homology, Amino Acid
- Tissue Distribution
- Xenopus
- Zebrafish
- PubMed
- 14701818 Full text @ J. Biol. Chem.
Citation
Robalino, J., Joshi, B., Fahrenkrug, S.C., and Jagus, R. (2004) Two zebrafish eIF4E family members are differentially expressed and functionally divergent. The Journal of biological chemistry. 279(11):10532-10541.
Abstract
Eukaryotic translation initiation factor 4E (eIF4E) is an essential component of the translational machinery that binds m7GTP and mediates the recruitment of capped mRNAs by the small ribosomal subunit. Recently, a number of proteins with homology to eIF4E have been reported in plants, invertebrates and mammals, that together with the prototypical translation factor constitute a new family of structurally related proteins. To distinguish the prototypical translation factor eIF4E from other family members, it has been termed eIF4E-1 (1). We describe the characterization of two eIF4E family members in the zebrafish Danio rerio. Based on their relative identities with human eIF4E-1 these zebrafish proteins are termed eIF4E-1A (82 %) and eIF4E-1B (66 %). eIF4E-1B, originally termed eIF4E(L), has previously been reported as the zebrafish eIF4E-1 counterpart (2,3). Comparison of the nucleotide sequences encoding the two proteins with human and Xenopus eIF4E-1 cDNAs, human genome sequences and completed invertebrate genome sequences suggests that the two genes probably evolved from a duplication event that occurred during vertebrate evolution. eIF4E-1A is expressed ubiquitously in zebrafish, while expression of eIF4E-1B is restricted to early embryonic development and to gonads and muscle of the tissues investigated. The ability of these two zebrafish proteins to bind m7GTP, eIF4G and 4E-BP, as well as to complement yeast conditionally deficient in functional eIF4E, show that eIF4E-1A is a functional equivalent of human eIF4E-1. Surprisingly, although eIF4E-1B possesses all known residues thought to be required for interaction with the cap-structure, eIF4G, and 4E-BPs, it fails to interact with any of these components suggesting that this protein serves a role other than that assigned to eIF4E.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping