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Splicing of a non‐canonical class three intein from Clostridium thermocellum
Author(s) -
Pusztay Jennifer M.,
Drago Matthew J.,
Powers Taryn L.,
Schufreider Ann K.,
Connor Katherine R.,
Reitter Julie N.,
Mills Kenneth V.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.789.5
Subject(s) - intein , protein splicing , rna splicing , chemistry , peptide bond , biochemistry , genetics , biology , peptide , gene , rna
Protein splicing is a post‐translational event by which an intervening polypeptide, called an intein, facilitates its own excision from the flanking polypeptides, called the exteins, and the ligation of the exteins. The first step of protein splicing is an amide to ester or thioester rearrangement of the peptide bond linking the N‐extein and intein, facilitated by the N‐terminal Ser or Cys of the intein. The Clostridium thermocellum TerA protein is interrupted by an intein that lacks the N‐terminal nucleophile. The TerA intein splices as a class three intein by bypassing the first step in the protein splicing mechanism and using an internal Cys to facilitate attack at the N‐terminal splice junction. We have examined the influence of conserved residues on the catalysis of this alternative mechanism. This material is based upon work supported by the National Science Foundation under grant MCB‐0950245 and the Camille and Henry Dreyfus Foundation.