This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kannan, T. R.
Right arrow Articles by Baseman, J. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kannan, T. R.
Right arrow Articles by Baseman, J. B.

 Previous Article  |  Next Article 

Infection and Immunity, November 2008, p. 5082-5092, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00698-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of a Unique ClpB Protein of Mycoplasma pneumoniae and Its Impact on Growth{triangledown}

T. R. Kannan, Oxana Musatovova, Pramod Gowda, and Joel B. Baseman*

Department of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, Texas 78229-3900

Received 3 June 2008/ Returned for modification 24 July 2008/ Accepted 1 September 2008

Mycoplasma pneumoniae accounts for 20 to 30% of all community-acquired pneumonia and has been associated with other airway pathologies, including asthma, and a range of extrapulmonary manifestations. Although the entire genomic sequence of M. pneumoniae has been completed, the functions of many of these genes in mycoplasma physiology are unknown. In this study, we focused on clpB, a well-known heat shock gene in other bacteria, to examine its role in mycoplasma growth. Transcriptional and translational analyses of heat shock in M. pneumoniae indicated that clpB is significantly upregulated, reinforcing its status as a critical responder to heat stress. Interestingly, M. pneumoniae ClpB does not use dual translational start points for ClpB synthesis, like other ClpB-characterized bacteria. Biochemical characterization of purified M. pneumoniae recombinant ClpB revealed casein- and lysine-independent ATPase activity and DnaK-DnaJ-GrpE-dependent chaperone activity. An M. pneumoniae mini-Tn4001-integrated, clpB-null mutant was impaired in its ability to replicate under permissive growth conditions, demonstrating the growth-promoting status of ClpB.


* Corresponding author. Mailing address: Department of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900. Phone: (210) 567-3939. Fax: (210) 567-6491. E-mail: baseman{at}uthscsa.edu

{triangledown} Published ahead of print on 8 September 2008.

Editor: A. Camilli


Infection and Immunity, November 2008, p. 5082-5092, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00698-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.