| Autor: |
Tulum I; Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka, 558-8585, Japan., Kimura K; Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka, 558-8585, Japan., Miyata M; Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka, 558-8585, Japan. miyata@sci.osaka-cu.ac.jp. |
| Jazyk: |
angličtina |
| Zdroj: |
Scientific reports [Sci Rep] 2020 Mar 02; Vol. 10 (1), pp. 3792. Date of Electronic Publication: 2020 Mar 02. |
| DOI: |
10.1038/s41598-020-60535-z |
| Abstrakt: |
Mycoplasma mobile, a fish pathogen, exhibits its own specialized gliding motility on host cells based on ATP hydrolysis. The special protein machinery enabling this motility is composed of surface and internal protein complexes. Four proteins, MMOBs 1630, 1660, 1670, and 4860 constitute the internal complex, including paralogs of F-type ATPase/synthase α and β subunits. In the present study, the cellular localisation for the candidate gliding machinery proteins, MMOBs 1620, 1640, 1650, and 5430 was investigated by using a total internal reflection fluorescence microscopy system after tagging these proteins with the enhanced yellow fluorescent protein (EYFP). The M. mobile strain expressing a fusion protein MMOB1620-EYFP exhibited reduced cell-binding activity and a strain expressing MMOB1640 fused with EYFP exhibited increased gliding speed, showing the involvement of these proteins in the gliding mechanism. Based on the genomic sequences, we analysed the sequence conservativity in the proteins of the internal and the surface complexes from four gliding mycoplasma species. The proteins in the internal complex were more conserved compared to the surface complex, suggesting that the surface complex undergoes modifications depending on the host. The analyses suggested that the internal gliding complex was highly conserved probably due to its role in the motility mechanism. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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