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Trans-splicing of an artificially split fungal mini-intein
ISSN
0006-291X
Date Issued
2007
Author(s)
Elleuche, Skander
DOI
10.1016/j.bbrc.2007.02.035
Abstract
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 PRPS intein. Two of the sites introduced allowed splicing to occur in trans while the third was not functional. (c) 2007 Elsevier Inc. All rights reserved.