Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications

Inteins self-splice from precursor polypeptides to reconstitute functional proteins. Here we describe inteins as redox-responsive switches in bacteria. Regulation was achieved by engineering a disulfide bond between the intein’s catalytic cysteine and the flanking polypeptide. This interaction was v...

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Autores principales: Callahan, Brian P., Topilina, Natalya I., Stanger, Matthew J., Roey, Patrick Van, Belfort, Marlene
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087850/
https://www.ncbi.nlm.nih.gov/pubmed/21460844
http://dx.doi.org/10.1038/nsmb.2041
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author Callahan, Brian P.
Topilina, Natalya I.
Stanger, Matthew J.
Roey, Patrick Van
Belfort, Marlene
author_facet Callahan, Brian P.
Topilina, Natalya I.
Stanger, Matthew J.
Roey, Patrick Van
Belfort, Marlene
author_sort Callahan, Brian P.
collection PubMed
description Inteins self-splice from precursor polypeptides to reconstitute functional proteins. Here we describe inteins as redox-responsive switches in bacteria. Regulation was achieved by engineering a disulfide bond between the intein’s catalytic cysteine and the flanking polypeptide. This interaction was validated by an X-ray structure, which includes a transient splice junction. A natural analogue of the designed system was identified in Pyrococcus abysii, suggesting an unprecedented form of adaptive, post-translational regulation.
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spelling pubmed-30878502011-11-01 Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications Callahan, Brian P. Topilina, Natalya I. Stanger, Matthew J. Roey, Patrick Van Belfort, Marlene Nat Struct Mol Biol Article Inteins self-splice from precursor polypeptides to reconstitute functional proteins. Here we describe inteins as redox-responsive switches in bacteria. Regulation was achieved by engineering a disulfide bond between the intein’s catalytic cysteine and the flanking polypeptide. This interaction was validated by an X-ray structure, which includes a transient splice junction. A natural analogue of the designed system was identified in Pyrococcus abysii, suggesting an unprecedented form of adaptive, post-translational regulation. 2011-04-03 2011-05 /pmc/articles/PMC3087850/ /pubmed/21460844 http://dx.doi.org/10.1038/nsmb.2041 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Callahan, Brian P.
Topilina, Natalya I.
Stanger, Matthew J.
Roey, Patrick Van
Belfort, Marlene
Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title_full Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title_fullStr Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title_full_unstemmed Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title_short Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
title_sort structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087850/
https://www.ncbi.nlm.nih.gov/pubmed/21460844
http://dx.doi.org/10.1038/nsmb.2041
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