title: Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications.
abstract: 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.
authors: Wadsworth Center, New York State Department of Health, Albany, New York, USA.
authors: Brian P
authors: BP
authors: Callahan
authors: Natalya I
authors: NI
authors: Topilina
authors: Matthew J
authors: MJ
authors: Stanger
authors: Patrick
authors: P
authors: Van Roey
authors: Marlene
authors: M
authors: Belfort
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D018360:Crystallography, X-Ray; D004258:DNA Polymerase III / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D047669:Exteins / Q000235:genetics; D047668:Inteins / Q000235:genetics* / Q000502:physiology; D008958:Models, Molecular; D010084:Oxidation-Reduction; D019154:Protein Splicing; D046939:Synechocystis
chemical_list: D001426:Bacterial Proteins; C074904:DNA polymerase III, alpha subunit; D004258:DNA Polymerase III