Part:BBa_K3889069
porcine teschovirus-1 P2A Peptide Linker
P2A is a porcine teschovirus-1 derived self-cleavage 2A peptide. Compared to other 2A self-cleaving peptides, P2A has been shown to have relatively higher efficiency.
P2A linker works by ribosome skipping mechanism, that is, while translation is taking place, the ribosome skips an amino acid at the P2A linker site, thereby effectively separating the upstream protein from the downstream protein.
Due to these abilities, 2A Linkers can be effectively used as a small size replacement for IRES (Internal Ribosomal Entry Sites) while designing DNA sequences for recombinant protein (non-fused) in both prokaryotic and eukaryotic systems. Hence, this is a great tool for synthetic biology.
This is a modified version of BBa_K1442039 specific to our project's assembly. BsmBI recognition site was removed for Golden Gate compatibility.
Usage and Biology
We planned to use this linker in BBa_K3889100, BBa_K3889101, BBa_K3889102, BBa_K3889110, BBa_K3889112, BBa_K3889120 and BBa_K3889122 in order to coexpress fluorescent proteins to report protein production.
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]
References
1] Kim, J. H., Lee, S.-R., Li, L.-H., Park, H.-J., Park, J.-H., Lee, K. Y., Kim, M.-K., Shin, B. A., & Choi, S.-Y. (2011). High Cleavage Efficiency of a 2A Peptide Derived from Porcine Teschovirus-1 in Human Cell Lines, Zebrafish and Mice. In V. Thiel (Ed.), PLoS ONE (Vol. 6, Issue 4, p. e18556). Public Library of Science (PLoS). https://doi.org/10.1371/journal.pone.0018556
2] Liu, Z., Chen, O., Wall, J. B. J., Zheng, M., Zhou, Y., Wang, L., Ruth Vaseghi, H., Qian, L., & Liu, J. (2017). Systematic comparison of 2A peptides for cloning multi-genes in a polycistronic vector. In Scientific Reports (Vol. 7, Issue 1). Springer Science and Business Media LLC. https://doi.org/10.1038/s41598-017-02460-2
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