Hypusine-containing protein eIF5A promotes translation elongation

Preeti Saini, Daniel E. Eyler, Rachel Green and Thomas E. Dever ()
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Preeti Saini: Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA
Daniel E. Eyler: Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Rachel Green: Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Thomas E. Dever: Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA

Nature, 2009, vol. 459, issue 7243, 118-121

Abstract: A third elongation factor Various factors associate with the ribosome to assist in initiation, elongation and termination. Textbook accounts of protein synthesis describe just two universally conserved translation elongation factors — EF-Tu/eEF1A and EF-G/eEF2. Now a study of protein synthesis in the yeast Saccharomyces cerevisiae repositions a factor previously thought to be associated with the initiation process, eIF5A, as a central player in elongation. eIF5A is unusual in that it contains a rare amino acid, hypusine, that is required for its ability to stimulate elongation. Based on the defects observed in the absence of eIF5A, it is proposed that the factor may function with eEF2 in the translocation step.

Date: 2009
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DOI: 10.1038/nature08034

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