ArticleJournal of bacteriology2006
Morphology of isolated Gli349, a leg protein responsible for Mycoplasma mobile gliding via glass binding, revealed by rotary shadowing electron microscopy.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- A lytic transglycosylase connects bacterial focal adhesion complexes to the peptidoglycan cell wall.eLife · 2024Article
- A lytic transglycosylase connects bacterial focal adhesion complexes to the peptidoglycan cell wall.bioRxiv : the preprint server for biology · 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
- Motility Assays of Mycoplasma mobile Under Light Microscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Chained Structure of Dimeric FmBio · 2021Article
- Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy.mBio · 2021Article
- Force and Stepwise Movements of Gliding Motility in Human Pathogenic BacteriumFrontiers in microbiology · 2021Article
- Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile.Scientific reports · 2020Article
- Article
- Insights into the mechanism of ATP-driven rotary motors from direct torque measurement.Biophysical reviews · 2019Review
- Identification of novel protein domain for sialyloligosaccharide binding essential to Mycoplasma mobile gliding.FEMS microbiology letters · 2019Article
- Linear motor driven-rotary motion of a membrane-permeabilized ghost in Mycoplasma mobile.Scientific reports · 2018Article
- Detailed Analyses of Stall Force Generation in Mycoplasma mobile Gliding.Biophysical journal · 2018Article
- Structural Study of MPN387, an Essential Protein for Gliding Motility of a Human-Pathogenic Bacterium, Mycoplasma pneumoniae.Journal of bacteriology · 2016Article
- Novel mechanisms power bacterial gliding motility.Molecular microbiology · 2016Review
- Article
- Gliding Direction of Mycoplasma mobile.Journal of bacteriology · 2016Article
- Gliding Motility of Mycoplasma mobile on Uniform Oligosaccharides.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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