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Protein translocation

Slowly (translate) but surely (translocate)

Nature Reviews Molecular Cell Biology volume 16, pages 2–3 (2015)Cite this article

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An Erratum to this article was published on 18 December 2014

This article has been updated

recognition by the SRP is enhanced by downstream non-optimal codons

The Frydman research group had previously produced data on SRP interactions in yeast cells and found a high degree of SRP selectivity in vivo to hydrophobic amino-terminal signal sequences and transmembrane domains in nascent polypeptides. Using this data set, the authors analysed proteins containing signal sequences with different SRP interaction enrichments, and found that the intrinsic sequence and structure properties of the signal sequences were not major determinants of SRP selectivity. Considering that the SRP binds to substrates co-translationally, the authors examined whether local translation elongation rates could have a role in SRP selectivity. They found that the mRNAs of the stronger SRP substrates, but not those of weaker ones, contain conserved regions of non-optimal codons positioned at ∼38–43 codons downstream of the start of the signal sequence, a position that is optimal for slowing elongation just as the signal sequence emerges from the ribosome. Notably, this is a local effect, as the stronger SRP substrates exhibit overall high translation efficiencies. This indicates that such sequence features have evolved to transiently slow translation elongation to improve nascent chain recognition by the SRP. The authors proposed calling such sequences (m)RNA-encoded slowdown of translation (REST).

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Change history

  • 18 December 2014

    The last sentence of the penultimate paragraph stated that the efficiency of translation decreased when a REST sequence was changed to optimal codons. It should have stated that the efficiency of translocation decreased in this setting. This has now been corrected online. The editors apologize for any confusion caused.

References

  1. Pechmann, S., Chartron, J.W. & Frydman J. Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nature Struct. Mol. Biol. http://dx.doi.org/10.1038/nsmb.2919 (2014)

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  1. Eytan Zlotorynski
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Hegde, R.S. & Keenan, R.J. Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nature Rev. Mol. Cell Biol. 12, 787–798 (2011)

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Zlotorynski, E. Slowly (translate) but surely (translocate). Nat Rev Mol Cell Biol 16, 2–3 (2015). https://doi.org/10.1038/nrm3921

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