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Please use this identifier to cite or link to this item: http://hdl.handle.net/10023/2227
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Title: 2A peptides provide distinct solutions to driving stop-carry on translational recoding
Authors: Sharma, P
Yan, F
Doronina, V
Escuin-Ordinas, Helena
Ryan, Martin Denis
Brown, Jeremy
Keywords: QP Physiology
Issue Date: Apr-2012
Citation: Sharma , P , Yan , F , Doronina , V , Escuin-Ordinas , H , Ryan , M D & Brown , J 2012 , ' 2A peptides provide distinct solutions to driving stop-carry on translational recoding ' Nucleic Acids Research , vol 40 , no. 7 , pp. 3143-3151 .
Abstract: Expression of viral proteins frequently includes non-canonical decoding events (‘recoding’) during translation. ‘2A’ oligopeptides drive one such event, termed ‘stop-carry on’ recoding. Nascent 2A peptides interact with the ribosomal exit tunnel to dictate an unusual stop codon-independent termination of translation at the final Pro codon of 2A. Subsequently, translation ‘reinitiates’ on the same codon, two individual proteins being generated from one open reading frame. Many 2A peptides have been identified, and they have a conserved C-terminal motif. Little similarity is present in the N-terminal portions of these peptides, which might suggest that these amino acids are not important in the 2A reaction. However, mutagenesis indicates that identity of the amino acid at nearly all positions of a single 2A peptide is important for activity. Each 2A may then represent a specific solution for positioning the conserved C-terminus within the peptidyl-transferase centre to promote recoding. Nascent 2A peptide:ribosome interactions are suggested to alter ribosomal fine structure to discriminate against prolyl-tRNAPro and promote termination in the absence of a stop codon. Such structural modifications may account for our observation that replacement of the final Pro codon of 2A with any stop codon both stalls ribosome processivity and inhibits nascent chain release.
Version: Publisher PDF
Description: Funded by the U.K. Biotechnology and Biological Sciences Research Council (BB/E/01070911)
Status: Peer reviewed
URI: http://hdl.handle.net/10023/2227
DOI: http://dx.doi.org/10.1093/nar/gkr1176
ISSN: 0305-1048
Type: Journal article
Rights: © The Author(s) 2011. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Appears in Collections:University of St Andrews Research
Biology Research
Biomedical Sciences Research Complex (BSRC) Research



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