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

Nikolay Burnaevskiy, Thomas G. Fox, Daniel A. Plymire, James M. Ertelt, Bethany A. Weigele, Andrey S. Selyunin, Sing Sing Way, Steven M. Patrie and Neal M. Alto ()
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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

Nature, 2013, vol. 496, issue 7443, 106-109

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.

Date: 2013
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DOI: 10.1038/nature12004

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