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
Google Scholar
Right arrow Articles by Bose, S. R.
Right arrow Articles by Krause, D. C.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bose, S. R.
Right arrow Articles by Krause, D. C.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2009, p. 6741-6748, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.01486-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mycoplasma pneumoniae Cytoskeletal Protein HMW2 and the Architecture of the Terminal Organelle{triangledown}

Stephanie R. Bose,{dagger} Mitchell F. Balish,{ddagger} and Duncan C. Krause*

Department of Microbiology, University of Georgia, Athens, Georgia 30602

Received 22 October 2008/ Accepted 24 August 2009

The terminal organelle of Mycoplasma pneumoniae mediates cytadherence and gliding motility and functions in cell division. The defining feature of this complex membrane-bound cell extension is an electron-dense core of two segmented rods oriented longitudinally and enlarging to form a bulb at the distal end. While the components of the core have not been comprehensively identified, previous evidence suggested that the cytoskeletal protein HMW2 forms parallel bundles oriented lengthwise to yield the major rod of the core. In the present study, we tested predictions emerging from that model by ultrastructural and immunoelectron microscopy analyses of cores from wild-type M. pneumoniae and mutants producing HMW2 derivatives. Antibodies specific for the N or C terminus of HMW2 labeled primarily peripheral to the core along its entire length. Furthermore, truncation of HMW2 did not correlate specifically with core length. However, mutant analysis correlated specific HMW2 domains with core assembly, and examination of core-enriched preparations confirmed that HMW2 was a major component of these fractions. Taken together, these findings yielded a revised model for HMW2 in terminal organelle architecture.

* Corresponding author. Mailing address: Department of Microbiology, 019 Riverbend Research South, 220 Riverbend Road, University of Georgia, Athens, GA 30602. Phone: (706) 542-2671. Fax: (706) 542-3804. E-mail: dkrause{at}uga.edu

{triangledown} Published ahead of print on 28 August 2009.

{dagger} Present address: Department of Biology, University of Nebraska at Omaha, Omaha, NE.

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

Journal of Bacteriology, November 2009, p. 6741-6748, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.01486-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»