2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe .
| Autor: | Ren Y; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, United States.; Nanobiology Institute, Yale University, West Haven, Connecticut, United States., Lin Q; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, United States.; Nanobiology Institute, Yale University, West Haven, Connecticut, United States., Berro J; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, United States.; Nanobiology Institute, Yale University, West Haven, Connecticut, United States.; Department of Cell Biology, Yale University, New Haven, Connecticut, United States. |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | MicroPublication biology [MicroPubl Biol] 2023 Sep 11; Vol. 2023. Date of Electronic Publication: 2023 Sep 11 (Print Publication: 2023). |
| DOI: | 10.17912/micropub.biology.000941 |
| Abstrakt: | 2A peptides are widely used for polycistronic gene expression from vectors. In contrast, the separation of endogenous genes via 2A peptides has been largely unexplored. We show that in fission yeast Schizosaccharomyces pombe , the "cleaving" efficiency of the 2A peptide from ERBV-1 (Equine rhinitis B virus 1) range from ~70% to ~99% for End4 at different insertion sites. Our results suggest a high "cleaving" efficiency as well as considerable variation for using 2A peptide to separate endogenous protein domains in fission yeast. Verification of the "cleaving" efficiency of 2A peptides is advised for its application. Competing Interests: The authors declare that there are no conflicts of interest present. (Copyright: © 2023 by the authors.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|