Related Experiment Video
Updated: Mar 21, 2026

Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
Published on: May 10, 2018
'2A-Like' Signal Sequences Mediating Translational Recoding: A Novel Form of Dual Protein Targeting
Claire Roulston1, Garry A Luke1, Pablo de Felipe2
1Biomolecular Sciences Building, University of St Andrews, North Haugh, St Andrews, Fife, KY16 9ST, Scotland, UK.
Abstract:
We report the initial characterization of an N-terminal oligopeptide '2A-like' sequence that is able to function both as a signal sequence and as a translational recoding element. Owing to this translational recoding activity, two forms of nascent polypeptide are synthesized: (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 synthesized as a separate translation product and, therefore, the nascent (downstream) polypeptide lacks the 2A-like signal sequence and is localized 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.
Related Concept Videos
Directing Proteins to the Rough Endoplasmic Reticulum
Leaky Scanning
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Signal Sequences and Sorting Receptors
Regulated mRNA Transport
Regulated mRNA Transport

