| Literature DB >> 24912194 |
Yoshiaki Kinosita1, Daisuke Nakane2, Mitsuhiro Sugawa1, Tomoko Masaike3, Kana Mizutani1, Makoto Miyata4, Takayuki Nishizaka5.
Abstract
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 μm⋅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.Entities:
Keywords: F1-ATPase; bacteria tracking; gliding ghost; leg protein; pairwise distance function
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Year: 2014 PMID: 24912194 PMCID: PMC4060671 DOI: 10.1073/pnas.1310355111
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205