ArticleProceedings of the National Academy of Sciences of the United States of America2007
Cytoskeletal "jellyfish" structure of Mycoplasma mobile.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Insights in tubulin-like structures of the poultry pathogen Mycoplasmoides gallisepticum.Archives of microbiology · 2026Article
- Distinct motors, shared mechanics: unifying principles of microbial gliding.Journal of bacteriology · 2026Review
- An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas.PLoS pathogens · 2026Article
- Unraveling the role of distinct cytoskeletal motility structures in Mycoplasma pneumoniae relatives.BMC microbiology · 2025Review
- Dimeric assembly of FScience advances · 2025Article
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Gliding direction ofBiophysics and physicobiology · 2025Article
- Rapid in vitro method to assemble and transfer DNA fragments into the JCVI-syn3B minimal synthetic bacterial genome through Cre/Biophysics and physicobiology · 2024Article
- Internal structure ofBiophysics and physicobiology · 2024Article
- Structure and Function of Gli123 Involved in Mycoplasma mobile Gliding.Journal of bacteriology · 2023Article
- Detection of Steps and Rotation in the Gliding Motility of Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Purification and Structural Analysis of the Gliding Motility Machinery in Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cell shape controls rheotaxis in small parasitic bacteria.PLoS pathogens · 2022Article
- Imaging Minimal Bacteria at the Nanoscale: a Reliable and Versatile Process to Perform Single-Molecule Localization Microscopy in Mycoplasmas.Microbiology spectrum · 2022Article
- Isolation and structure of the fibril protein, a major component of the internal ribbon forFrontiers in microbiology · 2022Article
- Traditional protocols and optimization methods lead to absent expression in a mycoplasma cell-free gene expression platform.Synthetic biology (Oxford, England) · 2022Article
- Chained Structure of Dimeric FmBio · 2021Article
- Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy.mBio · 2021Article
- Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile.Scientific reports · 2020Article
- Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma mobile, a parasitic bacterium lacking a peptidoglycan layer, glides on solid surfaces in the direction of a membrane protrusion at a cell pole by a unique mechanism. Recently, we proposed a working model in which cells are propelled by leg proteins clustering at the protrusion's base. The legs repeatedly catch and release sialic acids on the solid surface, a motion that is driven by the force generated by ATP hydrolysis. Here, to clarify the subcellular structure supporting the gliding force and the cell shape, we stripped the membrane by Triton X-100 and identified a unique structure, designated the "jellyfish" structure. In this structure, an oval solid "bell" approximately 235 wide and 155 nm long is filled with a 12-nm hexagonal lattice and connected to this structure are dozens of flexible "tentacles" that are covered with particles of 20-nm diameter at intervals of approximately 30 nm. The particles appear to have 180 degrees rotational symmetry and a dimple at the center. The relation of this structure to the gliding mechanism was suggested by its cellular localization and by analyses of mutants lacking proteins essential for gliding. We identified 10 proteins as the components by mass spectrometry and found that these do not show sequence similarities with other proteins of bacterial cytoskeletons or the gliding proteins previously identified. Immunofluorescence and immunoelectron microscopy revealed that two components are localized at the bell and another that has the structure similar to the F(1)-ATPase beta subunit is localized at the tentacles.
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