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Translation Elongation Factor-III (EP-3) - an Evolving Eukaryotic Ribosomal-Protein

Belfield, G.P, Rosssmith, N.J., Tuite, Mick F. (1995) Translation Elongation Factor-III (EP-3) - an Evolving Eukaryotic Ribosomal-Protein. Journal of Molecular Evolution, 41 (3). pp. 376-387. ISSN 0022-2844. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:19700)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.


Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), exhibits ribosome-dependent ATPase and GTPase activities that are not intrinsic to the fungal ribosome but are nevertheless essential for translation elongation in vivo. The EF-3 polypeptide has been identified in a wide range of fungal species and the gene encoding EF-3 (YEF3) has been isolated from four fungal species (Saccharomyces cerevisiae, Candida albicans, Candida guillermondii, and Pneumocystis carinii). Computer-assisted analysis of the predicted S. cerevisiae EF-3 amino acid sequence was used to identify several potential functional domains; two ATP binding/catalytic domains conserved with equivalent domains in members of the ATP-Binding Cassette (ABC) family of proteins, an amino-terminal region showing significant similarity to the E. coli S5 ribosomal protein, and regions of predicted interaction with rRNA, tRNA, and mRNA. Furthermore, EF-3 was also found to display amino acid similarity to myosin proteins whose cellular function is to provide the motive force of muscle. The identification of these regions provides clues to both the evolution and function of EF-3. The predicted functional regions are conserved among all known fungal EF-3 proteins and a recently described homologue encoded by the Chlorella virus CVK2. We propose that EF-3 may play a role in the ribosomal optimization of the accuracy of fungal protein synthesis by altering the conformation and activity of a ribosomal ''accuracy center,'' which is equivalent to the S4-S5-S12 ribosomal protein accuracy center domain of the E. coli ribosome. Furthermore, we suggest that EF-3 represents an evolving ribosomal protein with properties analogous to the intrinsic ATPase activities of higher eukaryotic ribosomes, which has wider implications for the evolutionary divergence of fungi from other eukaryotes.

Item Type: Article
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: P. Ogbuji
Date Deposited: 08 Jun 2009 11:09 UTC
Last Modified: 16 Nov 2021 09:57 UTC
Resource URI: (The current URI for this page, for reference purposes)

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