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Journal of Bacteriology, April 2006, p. 2821-2828, Vol. 188, No. 8
0021-9193/06/$08.00+0     doi:10.1128/JB.188.8.2821-2828.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Morphology of Isolated Gli349, a Leg Protein Responsible for Mycoplasma mobile Gliding via Glass Binding, Revealed by Rotary Shadowing Electron Microscopy

Jun Adan-Kubo,1 Atsuko Uenoyama,1 Toshiaki Arata,2 and Makoto Miyata1,3*

Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan,1 Department of Biological Sciences, Graduate School of Science and CREST/Japan Science and Technology Agency, Osaka University, Toyonaka, Osaka 560-0043, Japan,2 PRESTO, Japan Science and Technology Agency, Sumiyoshi-ku, Osaka 558-8585, Japan3

Received 9 December 2005/ Accepted 18 January 2006

Several species of mycoplasmas rely on an unknown mechanism to glide across solid surfaces in the direction of a membrane protrusion at the cell pole. Our recent studies on the fastest species, Mycoplasma mobile, suggested that a 349-kDa protein, Gli349, localized at the base of the membrane protrusion called the neck, forms legs that stick out from the neck and propel the cell by repeatedly binding to and releasing from a solid surface, based on the energy of ATP hydrolysis. Here, the Gli349 protein was isolated from mycoplasma cells and its structure was analyzed. Gel filtration analysis showed that the isolated Gli349 protein is monomeric. Rotary shadowing electron microscopy revealed that the molecular structure resembles the symbol for an eighth note in music. It contains an oval foot 14 nm long in axis. From this foot extend three rods in tandem of 43, 20, and 20 nm, in that order. The hinge connecting the first and second rods is flexible, while the next hinge has a distinct preference in its angle, near 90 degrees. Molecular images revealed that a monoclonal antibody that can bind to the position at one-third of the total peptide length from the N terminus bound to a position two-thirds from the foot end, suggesting that the foot corresponds to the C-terminal region. The amino acid sequence was assigned to the molecular image, and the topology of the molecule in the gliding machinery is discussed.

* Corresponding author. Mailing address: Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan. Phone: 81 (6) 6605 3157. Fax: 81 (6) 6605 3158. E-mail: miyata{at}sci.osaka-cu.ac.jp.

Journal of Bacteriology, April 2006, p. 2821-2828, Vol. 188, No. 8
0021-9193/06/$08.00+0     doi:10.1128/JB.188.8.2821-2828.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Nakane, D., Miyata, M. (2009). Cytoskeletal Asymmetrical Dumbbell Structure of a Gliding Mycoplasma, Mycoplasma gallisepticum, Revealed by Negative-Staining Electron Microscopy. J. Bacteriol. 191: 3256-3264 [Abstract] [Full Text]  
  • Uenoyama, A., Seto, S., Nakane, D., Miyata, M. (2009). Regions on Gli349 and Gli521 Protein Molecules Directly Involved in Movements of Mycoplasma mobile Gliding Machinery, Suggested by Use of Inhibitory Antibodies and Mutants. J. Bacteriol. 191: 1982-1985 [Abstract] [Full Text]  
  • Nakane, D., Miyata, M. (2007). Cytoskeletal "jellyfish" structure of Mycoplasma mobile. Proc. Natl. Acad. Sci. USA 104: 19518-19523 [Abstract] [Full Text]  
  • Nagai, R., Miyata, M. (2006). Gliding Motility of Mycoplasma mobile Can Occur by Repeated Binding to N-Acetylneuraminyllactose (Sialyllactose) Fixed on Solid Surfaces.. J. Bacteriol. 188: 6469-6475 [Abstract] [Full Text]  


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