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Journal of Bacteriology, March 2004, p. 1638-1647, Vol. 186, No. 6
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.6.1638-1647.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Temperature Regulation of the Hemin Storage (Hms+) Phenotype of Yersinia pestis Is Posttranscriptional

Robert D. Perry,* Alexander G. Bobrov, Olga Kirillina, Heather A. Jones,{dagger} Lisa Pedersen,{ddagger} Jennifer Abney, and Jacqueline D. Fetherston

Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, Kentucky 40536

Received 20 August 2003/ Accepted 29 November 2003

In Yersinia pestis, the Congo red (and hemin) binding that is characteristic of the Hms+ phenotype occurs at temperatures up to 34°C but not at higher temperatures. Manifestation of the Hms+ phenotype requires at least five proteins (HmsH, -F, -R, -S, and -T) that are organized into two separate operons: hmsHFRS and hmsT. HmsH and HmsF are outer membrane proteins, while HmsR, HmsS, and HmsT are predicted to be inner membrane proteins. We have used transcriptional reporter constructs, RNA dot blots, and Western blots to examine the expression of hms operons and proteins. Our studies indicate that transcription from the hmsHFRS and hmsT promoters is not regulated by the iron status of the cells, growth temperature, or any of the Hms proteins. In addition, the level of mRNA for both operons is not significantly affected by growth temperature. However, protein levels of HmsH, HmsR, and HmsT in cells grown at 37°C are very low compared to those in cells grown at 26°C, while the amounts of HmsF and HmsS show only a moderate reduction at the higher growth temperature. Neither the Pla protease nor a putative endopeptidase (Y2360) encoded upstream of hmsH is essential for temperature regulation of the Hms+ phenotype. However, HmsT at 37°C is sensitive to degradation by Lon and/or ClpPX. Thus, the stability of HmsH, HmsR, and HmsT proteins likely plays a role in temperature regulation of the Hms+ phenotype of Y. pestis.

* Corresponding author. Mailing address: Department of Microbiology, Immunology, and Molecular Genetics, MS415 Medical Center, University of Kentucky, Lexington, KY 40536-0298. Phone: (859) 323-6341. Fax: (859) 257-8994. E-mail: rperry{at}pop.uky.edu.

{dagger} Present address: Diversa, Corp., San Diego, CA 92121.

{ddagger} Present address: Palmer College of Chiropractic, Davenport, IA 52803.

Journal of Bacteriology, March 2004, p. 1638-1647, Vol. 186, No. 6
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.6.1638-1647.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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