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2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe

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...

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Detalles Bibliográficos
Autores principales: Ren, Yuan, Lin, Qun, Berro, Julien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520729/
https://www.ncbi.nlm.nih.gov/pubmed/37767365
http://dx.doi.org/10.17912/micropub.biology.000941
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author Ren, Yuan
Lin, Qun
Berro, Julien
author_facet Ren, Yuan
Lin, Qun
Berro, Julien
author_sort Ren, Yuan
collection PubMed
description 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.
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spelling pubmed-105207292023-09-27 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe Ren, Yuan Lin, Qun Berro, Julien MicroPubl Biol New Method 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. Caltech Library 2023-09-11 /pmc/articles/PMC10520729/ /pubmed/37767365 http://dx.doi.org/10.17912/micropub.biology.000941 Text en Copyright: © 2023 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle New Method
Ren, Yuan
Lin, Qun
Berro, Julien
2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title_full 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title_fullStr 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title_full_unstemmed 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title_short 2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast Schizosaccharomyces pombe
title_sort 2a peptide from erbv-1 efficiently separates endogenous protein domains in the fission yeast schizosaccharomyces pombe
topic New Method
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520729/
https://www.ncbi.nlm.nih.gov/pubmed/37767365
http://dx.doi.org/10.17912/micropub.biology.000941
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AT berrojulien 2apeptidefromerbv1efficientlyseparatesendogenousproteindomainsinthefissionyeastschizosaccharomycespombe