Difference between revisions of "Part:BBa K1442039"
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| − | The self-cleaving 2A peptide is a virally derived coding region that has been utilised by viruses to self-cleave during translation and is likely to have arisen to overcome traditional IRES sequences due to its much smaller coding length | + | The self-cleaving 2A peptide (18-22 amino acids) is a virally derived coding region that has been utilised by viruses to self-cleave during translation and is likely to have arisen to overcome traditional IRES sequences due to its much smaller coding length and allows for a smaller viral genome [1]. |
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| − | Of the available 2A coding regions coding for the peptide from various viruses: foot-and-mouth disease virus, equine rhinitis A, <i>Thosea asigna</i> | + | Of the available 2A coding regions coding for the peptide from various viruses: foot-and-mouth disease virus, equine rhinitis A, <i>Thosea asigna</i>, porcine teschovirus-1. The porcine teschovirus 2A (P2A) had the highest efficiency of cleavage in three mammalian cell lines tested by Kim et al [1]: human, zebrafish and adult mice. |
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| + | The P2A peptide can be used in a research context to allow multicistronic expression of genes without traditional methods of: multiple promoters, insertion of a splicing signal, insertion of a proteolytic cleavage site (e.g. TEV) and IRESs. Of note, P2A overcomes the limitations of an IRES: it is much smaller and also improves the translational efficiency of IRES-based genes. | ||
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Revision as of 07:11, 16 October 2014
P2A self-cleaving peptide sequence
The self-cleaving 2A peptide (18-22 amino acids) is a virally derived coding region that has been utilised by viruses to self-cleave during translation and is likely to have arisen to overcome traditional IRES sequences due to its much smaller coding length and allows for a smaller viral genome [1].
Of the available 2A coding regions coding for the peptide from various viruses: foot-and-mouth disease virus, equine rhinitis A, Thosea asigna, porcine teschovirus-1. The porcine teschovirus 2A (P2A) had the highest efficiency of cleavage in three mammalian cell lines tested by Kim et al [1]: human, zebrafish and adult mice.
The P2A peptide can be used in a research context to allow multicistronic expression of genes without traditional methods of: multiple promoters, insertion of a splicing signal, insertion of a proteolytic cleavage site (e.g. TEV) and IRESs. Of note, P2A overcomes the limitations of an IRES: it is much smaller and also improves the translational efficiency of IRES-based genes.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]