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Polypeptide ligation occurs during post-translational modification of concanavalin A

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Abstract

Lectins are proteins with multivalent carbohydrate-binding sites, which confer the ability to agglutinate. The seeds of legumes are particularly rich in lectins, for example, concanavalin A (Con A) comprises up to 15% of the protein in the cotyledons of jack bean (Canavalia ensiformis) seeds. The amino acid sequences of Con A and several other legume lectins have been partially or fully determined, and comparison of these sequences from different species reveals a circular homology1,2 (Fig. 1A); rearrangements within the genome have been suggested to explain this1,2. We report here that the circular homology displayed by Con A is due to a post-translational transposition and ligation within the initial poly-peptide. This type of modification has not been reported previously for eukaryotes, although it has been suggested to occur in bacteriophage λ (ref. 3).

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Authors and Affiliations

  1. Botany School, University of Cambridge, Downing Street, Cambridge, CB2 3EA, UK

    D. M. Carrington & D. E. Hanke

  2. SERC Protein Sequencing Unit, Department of Biochemistry, University of Leeds, 9 Hyde Terrace, Leeds, LS2 9LS, UK

    A. Auffret

Authors
  1. D. M. Carrington
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  2. A. Auffret
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  3. D. E. Hanke
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Carrington, D., Auffret, A. & Hanke, D. Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature 313, 64–67 (1985). https://doi.org/10.1038/313064a0

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  • DOI: https://doi.org/10.1038/313064a0

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