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Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ

Author

Listed:
  • Nikolay Burnaevskiy

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

  • Thomas G. Fox

    (Section of Pediatric Infectious Disease, Indiana University School of Medicine, 705 Riley Hospital Drive, ROC 4380, Indianapolis, Indiana 46202, USA)

  • Daniel A. Plymire

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

  • James M. Ertelt

    (Cincinnati Children’s Hospital Medical Center, 3333 Burnet Avenue, MLC 7017, Cincinnati, Ohio 45229-3039, USA)

  • Bethany A. Weigele

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

  • Andrey S. Selyunin

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

  • Sing Sing Way

    (Cincinnati Children’s Hospital Medical Center, 3333 Burnet Avenue, MLC 7017, Cincinnati, Ohio 45229-3039, USA)

  • Steven M. Patrie

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

  • Neal M. Alto

    (University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA)

Abstract

An irreversible mechanism of protein demyristoylation catalysed by invasion plasmid antigen J (IpaJ), a Shigella flexneri type III effector protein with cysteine protease activity, is described.

Suggested Citation

  • Nikolay Burnaevskiy & Thomas G. Fox & Daniel A. Plymire & James M. Ertelt & Bethany A. Weigele & Andrey S. Selyunin & Sing Sing Way & Steven M. Patrie & Neal M. Alto, 2013. "Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ," Nature, Nature, vol. 496(7443), pages 106-109, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7443:d:10.1038_nature12004
    DOI: 10.1038/nature12004
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