Ribosomal association of the yeast SAL4 (SUP45) gene product: implications for its role in translation fidelity and termination

Stansfield, Ian and Grant, Chris M. and Tuite, Mick F. (1992) Ribosomal association of the yeast SAL4 (SUP45) gene product: implications for its role in translation fidelity and termination. Molecular Microbiology, 6 (23). pp. 3469-3478. ISSN 0950-382X. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1111/j.1365-2958.1992.tb01782...

Abstract

The SAL4 gene of the yeast Saccharomyces cerevisiae encodes a novel translation factor (Sal4p) involved in maintaining translational fidelity. Using a polyclonal antibody raised against a Sal4p-beta-galactosidase fusion protein, Sal4p was shown to be almost exclusively associated with the ribosomal fraction. Even when the ribosomes were treated with 0.8 M KCl, only low levels of Sal4p were detected in the post-ribosomal supernatant, suggesting a very strong affinity between Sal4p and the ribosome. Analysis of the distribution of Sal4p in the ribosomal population revealed that it was principally associated with 40S subunits, monosomes and polysomes. Incubation in high salt concentrations (0.8 M KCl) suggested that the affinity of Sal4p for the 40S subunit was lower than that for monosomes or polysomes. The Sal4p:ribosome association was only maintained when ribosomes were prepared in the presence of the translation elongation inhibitor cycloheximide; in uninhibited cells much lower levels of Sal4p were detectable in the 'run-off' polysomes. In view of these data, and given the stoichiometry of Sal4p to individual ribosomal proteins (estimated at less than 1:20), we suggest that Sal4p plays an ancillary role in translation termination.

Item Type: Article
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: O.O. Odanye
Date Deposited: 03 Sep 2009 13:32
Last Modified: 10 Jun 2014 12:59
Resource URI: http://kar.kent.ac.uk/id/eprint/22242 (The current URI for this page, for reference purposes)
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