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Hypusine-containing protein eIF5A promotes translation elongation

Author

Listed:
  • 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)

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.

Suggested Citation

  • Preeti Saini & Daniel E. Eyler & Rachel Green & Thomas E. Dever, 2009. "Hypusine-containing protein eIF5A promotes translation elongation," Nature, Nature, vol. 459(7243), pages 118-121, May.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7243:d:10.1038_nature08034
    DOI: 10.1038/nature08034
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    Cited by:

    1. Saeede Salehi & Abdolhossein Zare & Gianluca Prezza & Jakob Bader & Cornelius Schneider & Utz Fischer & Felix Meissner & Matthias Mann & Michael Briese & Michael Sendtner, 2023. "Cytosolic Ptbp2 modulates axon growth in motoneurons through axonal localization and translation of Hnrnpr," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Yan Chen & Bin Tsai & Ningning Li & Ning Gao, 2022. "Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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