Initiation-Factor EIF-4E of Saccharomyces-Cerevisiae - Distribution Within the Cell, Binding to Messenger- RNA, and Consequences of its Overprodutction

Lang, V. and Zanchin, N.I.T and Lunsdorf, Heinrich and Tuite, Mick F. and McCarthy, John E. G. (1994) Initiation-Factor EIF-4E of Saccharomyces-Cerevisiae - Distribution Within the Cell, Binding to Messenger- RNA, and Consequences of its Overprodutction. Journal of Biological Chemistry, 269 (8). pp. 6117-6123. ISSN 0021-9258. (The full text of this publication is not available from this repository)

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Abstract

The eukaryotic translational initiation factor 4E (eIF-4E) is an essential protein that binds the 5' cap structure with high specificity and affinity. Yeast eIF-4E is homologous to eIF-4E of higher eukaryotes, but interacts with a different set of cap-binding complex proteins. In the present study the distribution of yeast eIF-4E in Saccharomyces cerevisiae was found to be similar to that observed in higher cells, whereby the yeast factor was more concentrated in the nucleus than in the cytoplasm. Overexpression of yeast eIF-4E in S. cerevisiae exerted at most a minimal effect on growth in liquid minimal medium and was not found to influence the translation of reporter gene mRNAs bearing secondary structure in their leader regions. In a new method to study mRNA-protein interactions, biotinylated mRNAs were synthesized in vitro for use in studies of the binding of eIF-4E in yeast extracts. Streptavidin was used to adsorb the biotinylated mRNAs plus bound initiation factors. Stem-loop structures in the leader region did not influence the binding of eIF-4E or, in comparative experiments, of eIF-4A Thus yeast eIF-4E shows both similarities and differences with respect to the distribution and function of its counterparts in higher eukaryotes.

Item Type: Article
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 25 Jun 2009 07:06
Last Modified: 15 Jul 2014 08:51
Resource URI: http://kar.kent.ac.uk/id/eprint/20299 (The current URI for this page, for reference purposes)
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