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Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile
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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7052211/ https://www.ncbi.nlm.nih.gov/pubmed/32123220 http://dx.doi.org/10.1038/s41598-020-60535-z |
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author | Tulum, Isil Kimura, Kenta Miyata, Makoto |
author_facet | Tulum, Isil Kimura, Kenta Miyata, Makoto |
author_sort | Tulum, Isil |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7052211 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-70522112020-03-06 Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile Tulum, Isil Kimura, Kenta Miyata, Makoto Sci Rep Article 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. Nature Publishing Group UK 2020-03-02 /pmc/articles/PMC7052211/ /pubmed/32123220 http://dx.doi.org/10.1038/s41598-020-60535-z Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Tulum, Isil Kimura, Kenta Miyata, Makoto Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title | Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title_full | Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title_fullStr | Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title_full_unstemmed | Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title_short | Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile |
title_sort | identification and sequence analyses of the gliding machinery proteins from mycoplasma mobile |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7052211/ https://www.ncbi.nlm.nih.gov/pubmed/32123220 http://dx.doi.org/10.1038/s41598-020-60535-z |
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