Trans-splicing of an artificially split fungal mini-intein.
Inteins are internal protein domains found inside the coding region of different proteins. They can autocatalytically self-excise from their host protein and ligate the protein flanks, called exteins, with a peptide bond via a post-translational process called protein cis-splicing. In contrast, protein trans-splicing involves inteins split into an N- and a C-terminal domain. Both domains are synthesized as two separate components and each joined to an extein; the intein domains can reassemble and link the joined exteins into one functional protein. In this study, we introduced three split sites into the PRP8 mini-intein of Penicillium chrysogenum and demonstrated for the first time trans-splicing of a fungal PRP8 intein. Two of the sites introduced allowed splicing to occur in trans while the third was not functional.
Elleuche
Skander
S
Institute of Microbiology and Genetics, Department of Genetics of Eukaryotic Microorganisms, Georg-August-University of Göttingen, Germany.
Pöggeler
Stefanie
S
D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D047668:Inteins / Q000235:genetics; D010408:Penicillium chrysogenum / Q000235:genetics / Q000378:metabolism*; D019154:Protein Splicing; D020040:Trans-Splicing
D005656:Fungal Proteins