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Updated: Jun 3, 2026

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia
Published on: September 12, 2025
Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
Brian P Callahan1, Natalya I Topilina, Matthew J Stanger
1Wadsworth Center, New York State Department of Health, Albany, New York, USA.
None:
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.
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