Initiation factor eIF-4E of Saccharomyces cerevisiae: distribution within the cell, binding to mRNA, and consequences of its overproduction

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 st...

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Bibliographic Details
Published in:The Journal of biological chemistry 1994-02, Vol.269 (8), p.6117-6123
Main Authors: Lang, V, Zanchin, N.I.T, Lunsdorf, H, Tuite, M, McCarthy, J.E.G
Format: Article
Language:English
Subjects:
ARN MENSAJERO
ARN MESSAGER
Base Sequence
BIOCHIMIE
Biological and medical sciences
BIOQUIMICA
CITOPLASMA
CYTOPLASME
DNA, Fungal - chemistry
DNA, Fungal - metabolism
Eukaryotic Initiation Factor-4E
Fundamental and applied biological sciences. Psychology
GENE
GENES
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
NOYAU CELLULAIRE
Nucleic Acid Conformation
NUCLEO
Peptide Initiation Factors - biosynthesis
Peptide Initiation Factors - metabolism
PROTEINAS AGLUTINANTES
PROTEINE DE LIAISON
RNA, Fungal
RNA, Messenger - chemistry
RNA, Messenger - metabolism
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - metabolism
Translation. Translation factors. Protein processing
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Summary: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
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(17)37577-4