Literature DB >> 9335286

The Mycobacterium xenopi GyrA protein splicing element: characterization of a minimal intein.

A Telenti1, M Southworth, F Alcaide, S Daugelat, W R Jacobs, F B Perler.   

Abstract

The 198-amino-acid in-frame insertion in the gyrA gene of Mycobacterium xenopi is the smallest known naturally occurring active protein splicing element (intein). Comparison with other mycobacterial gyrA inteins suggests that the M. xenopi intein underwent a complex series of events including (i) removal of 222 amino acids that encompass most of the central intein domain, and (ii) addition of a linker of unrelated residues. This naturally occurring genetic rearrangement is a representative characteristic of the taxon. The deletion process removes the conserved motifs involved in homing endonuclease activity. The linker insertion represents a structural requirement, as its mutation resulted in failure to splice. The M. xenopi GyrA intein thus provides a paradigm for a minimal protein splicing element.

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Year:  1997        PMID: 9335286      PMCID: PMC179553          DOI: 10.1128/jb.179.20.6378-6382.1997

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  19 in total

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Review 6.  The comings and goings of homing endonucleases and mobile introns.

Authors:  R F Doolittle
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-15       Impact factor: 11.205

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Authors:  F S Gimble; J Thorner
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  37 in total

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3.  Ribosomal Synthesis of Macrocyclic Peptides in Vitro and in Vivo Mediated by Genetically Encoded Aminothiol Unnatural Amino Acids.

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9.  Control of protein splicing by intein fragment reassembly.

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10.  Modular organization of inteins and C-terminal autocatalytic domains.

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