Abstract
The putative translation factor eIF5A is essential for cell viability and is highly conserved from archebacteria to mammals. Although this protein was originally identified as a translation initiation factor, subsequent experiments did not support a role for eIF5A in general translation. In this work, we demonstrate that eIF-5A interacts with structural components of the 80S ribosome, as well as with the translation elongation factor 2 (eEF2). Moreover, eIF5A is further shown to cofractionate with monosomes in a translation-dependent manner. Finally, eIF5A mutants show altered polysome profiles and are sensitive to translation inhibitors. Our results re-establish a function for eIF5A in translation and suggest a role for this factor in translation elongation instead of translation initiation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Eukaryotic Translation Initiation Factor 5A
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Lysine / analogs & derivatives
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Lysine / metabolism
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Mutation
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Peptide Chain Elongation, Translational
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Peptide Initiation Factors / chemistry
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Peptide Initiation Factors / genetics
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Peptide Initiation Factors / metabolism*
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Protein Biosynthesis*
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Protein Synthesis Inhibitors / pharmacology
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism*
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Ribosomes / metabolism
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Peptide Initiation Factors
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Protein Synthesis Inhibitors
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RNA-Binding Proteins
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Saccharomyces cerevisiae Proteins
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hypusine
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Lysine