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Publication Abstract from PubMed

Here we describe self-splicing proteins, called inteins, that function as redox-responsive switches in bacteria. Redox regulation was achieved by engineering a disulfide bond between the intein's catalytic cysteine and a cysteine in the flanking 'extein' sequence. This interaction was validated by an X-ray structure, which includes a transient splice junction. A natural analog of the designed system was identified in Pyrococcus abyssi, suggesting an unprecedented form of adaptive, post-translational regulation.

Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications.,Callahan BP, Topilina NI, Stanger MJ, Van Roey P, Belfort M Nat Struct Mol Biol. 2011 May;18(5):630-3. Epub 2011 Apr 3. PMID:21460844^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.