Minimization of a eukaryotic mini-intein.
Inteins are internal protein splicing elements that can autocatalytically self-excise from their host protein and ligate the protein flanks (exteins) with a peptide bond. Large inteins comprise independent protein splicing and endonuclease domains whereas mini-inteins lack the central endonuclease domain. To identify mini-intein domains that are essential for protein splicing, deletions were introduced at different sites of the 157-aa PRP8 mini-intein of Penicillium chrysogenum. The removal of eight and six amino acids at two different sites resulted in a functional eukaryotic mini-intein of only 143 aa.
Institute of Microbiology and Genetics, Department of Genetics of Eukaryotic Microorganisms, Georg-August-University of Göttingen, Grisebachstrasse 8, 37077 Gottingen, Germany.
Skander
S
Elleuche
Kristin
K
Döring
Stefanie
S
Pöggeler
D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics*; D047668:Inteins / Q000502:physiology*; D010408:Penicillium chrysogenum / Q000502:physiology*; D019154:Protein Splicing / Q000502:physiology*; D016601:RNA-Binding Proteins; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; C115374:PRPF8 protein, human; D016601:RNA-Binding Proteins