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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Willby, M. J.
Right arrow Articles by Krause, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Willby, M. J.
Right arrow Articles by Krause, D. C.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2004, p. 8221-8228, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8221-8228.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

HMW1 Is Required for Stability and Localization of HMW2 to the Attachment Organelle of Mycoplasma pneumoniae

Melisa J. Willby,{dagger} Mitchell F. Balish,{ddagger} Stephanie M. Ross, Kyungok K. Lee, Jarrat L. Jordan, and Duncan C. Krause*

Department of Microbiology, University of Georgia, Athens, Georgia

Received 29 June 2004/ Accepted 15 September 2004

The cytoskeletal proteins HMW1 and HMW2 are components of the terminal organelle of the cell wall-less bacterium Mycoplasma pneumoniae. HMW1 is required for a tapered, filamentous morphology but exhibits accelerated turnover in the absence of HMW2. Here, we report that a reciprocal dependency exists between HMW1 and HMW2, with HMW2 subject to accelerated turnover with the loss of HMW1. Furthermore, the instability of HMW2 correlated with its failure to localize to the attachment organelle. The C-terminal domain of HMW1 is essential for both function and its accelerated turnover in the absence of HMW2. We constructed HMW1 deletion derivatives lacking portions of this domain and examined each for stability and function. The C-terminal 41 residues were particularly important for proper localization and function in cell morphology and P1 localization, but the entire C-terminal domain was required to stabilize HMW2. The significance of these findings in the context of attachment organelle assembly is considered.


* Corresponding author. Mailing address: Department of Microbiology, 523 Biological Sciences Bldg., University of Georgia, Athens, GA 30602. Phone: (706) 542-2671. Fax: (706) 542-2674. E-mail: dkrause{at}uga.edu.

{dagger} Present address: Department of Microbiology and Immunology, Emory University, Atlanta, Ga.

{ddagger} Present address: Department of Microbiology, Miami University, Oxford, Ohio.


Journal of Bacteriology, December 2004, p. 8221-8228, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8221-8228.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Hasselbring, B. M., Krause, D. C. (2007). Proteins P24 and P41 Function in the Regulation of Terminal-Organelle Development and Gliding Motility in Mycoplasma pneumoniae. J. Bacteriol. 189: 7442-7449 [Abstract] [Full Text]  
  • Burgos, R., Pich, O. Q., Querol, E., Pinol, J. (2007). Functional Analysis of the Mycoplasma genitalium MG312 Protein Reveals a Specific Requirement of the MG312 N-Terminal Domain for Gliding Motility. J. Bacteriol. 189: 7014-7023 [Abstract] [Full Text]  
  • Hasselbring, B. M., Page, C. A., Sheppard, E. S., Krause, D. C. (2006). Transposon Mutagenesis Identifies Genes Associated with Mycoplasma pneumoniae Gliding Motility.. J. Bacteriol. 188: 6335-6345 [Abstract] [Full Text]  
  • Waldo, R. H. III, Krause, D. C. (2006). Synthesis, Stability, and Function of Cytadhesin P1 and Accessory Protein B/C Complex of Mycoplasma pneumoniae. J. Bacteriol. 188: 569-575 [Abstract] [Full Text]  
  • Uenoyama, A., Miyata, M. (2005). Identification of a 123-Kilodalton Protein (Gli123) Involved in Machinery for Gliding Motility of Mycoplasma mobile. J. Bacteriol. 187: 5578-5584 [Abstract] [Full Text]