"2A-like" signal sequences mediating translational recoding: a novel form of dual protein targeting

Claire Roulston, Garry Alec Luke, Pablo de Felipe, Lin Ruan, Jonathan Cope, John Nicholson, Andriy Sukhodub, Jens Tilsner, Martin Denis Ryan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)
3 Downloads (Pure)

Abstract

We report the initial characterisation of an N-terminal oligopeptide ‘2A-like’ sequence that is able to function both as a signal sequence and as a translational recoding element. Due to this translational recoding activity, two forms of nascent polypeptide are synthesised: (i) when 2A-mediated translational recoding has not occurred: the nascent polypeptide is fused to the 2A-like N-terminal signal sequence and the fusion translation product is targeted to the exocytic pathway, and, (ii) a translation product where 2A-mediated translational recoding has occurred: the 2A-like signal sequence is synthesised as a separate translation product and, therefore, the nascent (downstream) polypeptide lacks the 2A-like signal sequence and is localised to the cytoplasm. This type of dual-functional signal sequence results, therefore, in the partitioning of the translation products between the two sub-cellular sites and represents a newly described form of dual protein targeting.
Original languageEnglish
Pages (from-to)923-939
Number of pages17
JournalTraffic
Volume17
Issue number8
Early online date2 Jun 2016
DOIs
Publication statusPublished - 13 Jul 2016

Keywords

  • Translational recoding
  • 2A
  • Signal sequence
  • Secretory pathway
  • Dual protein targeting

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