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Comment
. 2017 Aug;42(8):587-588.
doi: 10.1016/j.tibs.2017.06.006. Epub 2017 Jun 29.

Breaking the Silos of Protein Synthesis

Maria K Mateyak  1 , Terri Goss Kinzy  2
Affiliations
Comment

Breaking the Silos of Protein Synthesis

Maria K Mateyak et al. Trends Biochem Sci. 2017 Aug.

Abstract

Protein synthesis requires factors that are proposed to enhance discrete steps. Eukaryotic initiation factor eIF5A was initially thought to affect initiation; however, it was later shown to facilitate translation elongation at polyproline. Recent work by Schuller et al. demonstrates that eIF5A facilitates both general elongation and termination in yeast, challenging these steps as silos.

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Figures

Figure 1
Figure 1
eIF5A functions at multiple steps of protein synthesis. While originally identified as enhancing the met-puromycin reaction in vitro, recent work demonstrates eIF5A stimulates general elongation as well as translation termination.
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Comment on

References

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    1. Gutierrez E, et al. eIF5A promotes translation of polyproline motifs. Mol Cell. 2013;51(1):35–45. - PMC - PubMed
    1. Saini P, et al. Hypusine-containing protein eIF5A promotes translation elongation. Nature. 2009;459(7243):118–21. - PMC - PubMed
    1. Ude S, et al. Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science. 2013;339(6115):82–5. - PubMed
    1. Doerfel LK, et al. EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science. 2013;339(6115):85–8. - PubMed

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