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 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.