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Infection and Immunity, November 2000, p. 6466-6471, Vol. 68, No. 11
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Yersinia pestis YscG Protein Is a Syc-Like Chaperone That Directly Binds YscE

James B. Day, Inna Guller, and Gregory V. Plano*

Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, Florida 33101

Received 21 June 2000/Returned for modification 25 July 2000/Accepted 3 August 2000

Pathogenic Yersinia species secrete virulence proteins, termed Yersinia outer proteins (Yops), upon contact with a eukaryotic cell. The secretion machinery is composed of 21 Yersinia secretion (Ysc) proteins. Yersinia pestis mutants defective in expression of YscG or YscE were unable to export the Yops. YscG showed structural and limited amino-acid-sequence similarities to members of the specific Yop chaperone (Syc) family of proteins. YscG specifically recognized and bound YscE; however, unlike previously characterized Syc substrates, YscE was not exported from the cell. These data suggest that YscG functions as a chaperone for YscE.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of Miami School of Medicine, P.O. Box 016960 (R-138), Miami, FL 33101. Phone: (305) 243-6310. Fax: (305) 243-4623. E-mail: gplano{at}med.miami.edu.

Infection and Immunity, November 2000, p. 6466-6471, Vol. 68, No. 11
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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