Translation elongation factor-III - A fungus-specific translation factor

Belfield, G.P and Tuite, Mick F. (1993) Translation elongation factor-III - A fungus-specific translation factor. Molecular Microbiology, 9 (3). pp. 411-418. ISSN 0950-382X. (The full text of this publication is not available from this repository)

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Abstract

Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), was first described in the yeast Saccharomyces cerevisiae and has subsequently been identified in a wide range of fungal species including Candida albicans and Schizo-saccharomyces pombe. EF-3 exhibits ribosome-dependent ATPase and GTPase activities that are not intrinsic to the fungal ribosome, but which are essential for translation elongation. Recent studies on the structure of EF-3 from several fungal species have shown that it consists of a repeated domain, with each domain containing the expected putative ATP- and GTP-binding motifs. Overall, EF-3 shows striking amino acid similarity to members of the ATP-binding Cassette (ABC) family of membrane-associated transport proteins although EF-3 is not itself directly membrane-associated. Regions of the EF-3 polypeptide also show structural homology with other translation-associated factors including aminoacyl-tRNA synthetases and the Escherichia coli ribosomal protein S5. While the precise role of EF-3 in the translation elongation cycle remains to be defined, recent evidence suggests that it may be involved in optimizing accuracy during mRNA decoding at the ribosomal A site. Furthermore, the essential nature of EF-3 with respect to the fungal cell indicates that it may be an effective antifungal target. Its apparently ubiquitous occurrence throughout the fungal kingdom also suggests that it may be a useful fungal taxonomic marker.

Item Type: Review
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: R.F. Xu
Date Deposited: 20 Oct 2009 21:08
Last Modified: 10 Jun 2014 12:52
Resource URI: http://kar.kent.ac.uk/id/eprint/20795 (The current URI for this page, for reference purposes)
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