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Journal of Bacteriology, April 2000, p. 1834-1843, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Yersinia pestis YscY Protein Directly Binds YscX, a Secreted Component of the Type III Secretion Machinery

James B. Day and Gregory V. Plano*

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

Received 26 August 1999/Accepted 10 January 2000

Human pathogenic yersiniae organisms export and translocate the Yop virulence proteins and V antigen upon contact with a eukaryotic cell. Yersinia pestis mutants defective for production of YscX or YscY were unable to export the Yops and V antigen. YscX and YscY were both present in the Y. pestis cell pellet fraction; however, YscX was also found in the culture supernatant. YscY showed structural and amino acid sequence similarities to the Syc family of proteins. YscY specifically recognized and bound to a region of YscX that included a predicted coiled-coil region. These data suggest that YscY may function as a chaperone for YscX in Y. pestis.

* 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.

Journal of Bacteriology, April 2000, p. 1834-1843, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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