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Genetic Definition of a Protein-Splicing Domain - Functional Mini-Inteins Support Structure Predictions and a Model For Intein Evolution

  1. Author:
    Derbyshire, V.
    Wood, D. W.
    Wu, W.
    Dansereau, J. T.
    Dalgaard, J. Z.
    Belfort, M.

  2. Author Address

    Belfort M NEW YORK STATE DEPT HLTH WADSWORTH CTR MOL GENET PROGRAM ALBANY, NY 12237 USA SUNY ALBANY SCH PUBL HLTH ALBANY, NY 12201 USA NEW YORK STATE DEPT HLTH WADSWORTH CTR MOL GENET PROGRAM ALBANY, NY 12237 USA RENSSELAER POLYTECH INST ISERMANN DEPT CHEM ENGN TROY, NY 12180 USA NCI FREDERICK CANC RES & DEV CTR ADV BIOSCI LABS BASIC RES PROGRAM FREDERICK, MD 21701 USA
    1. Year: 1997
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 94
    2. 21
    3. Pages: 11466-11471
  4. Type of Article: Article
  1. Abstract:

    Inteins are protein-splicing elements, most of which contain conserved sequence blocks that define a family of homing endonucleases. Like group I introns that encode such endonucleases, inteins are mobile genetic elements. Recent crystallography and computer modeling studies suggest that inteins consist of two structural domains that correspond to the endonuclease and the protein-splicing elements. To determine whether the bipartite structure of inteins is mirrored by the functional independence of the protein-splicing domain, the entire endonuclease component was deleted from the Mycobacterium tuberculosis recA intein. Guided by computer modeling studies, and taking advantage of genetic systems designed to monitor intein function, the 440-aa Mtu recA intein was reduced to a functional mini-intein of 137 aa. The accuracy of splicing of several mini-inteins was verified. This work not only substantiates structure predictions for intein function but also supports the hypothesis that, like group I introns, mobile inteins arose by an endonuclease gene invading a sequence encoding a small, functional splicing element. [References: 30]

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