Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 23, Pages 8601-8606Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1310355111
Keywords
bacteria tracking; gliding ghost; leg protein; pairwise distance function; F1-ATPase
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Funding
- Japan Society for the Promotion of Science [LR033]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [26103527, 25893230]
- Asahi Glass Foundation
- Institute for Fermentation
- Naito Foundation Natural Science Scholarship
- Grants-in-Aid for Scientific Research [25893230, 26103527, 24117002, 24390107, 25113524] Funding Source: KAKEN
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Among the bacteria that glide on substrate surfaces, Mycoplasma mobile is one of the fastest, exhibiting smooth movement with a speed of 2.0-4.5 mu m.s(-1) with a cycle of attachment to and detachment from sialylated oligosaccharides. To study the gliding mechanism at the molecular level, we applied an assay with a fluorescently labeled and membrane-permeabilized ghost model, and investigated the motility by high precision colocalization microscopy. Under conditions designed to reduce the number of motor interactions on a randomly oriented substrate, ghosts took unitary 70-nm steps in the direction of gliding. Although it remains possible that the stepping behavior is produced by multiple interactions, our data suggest that these steps are produced by a unitary gliding machine that need not move between sites arranged on a cytoskeletal lattice.
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