dc.contributor.author | Neuhaus, A | |
dc.contributor.author | Selvaraj, M | |
dc.contributor.author | Salzer, R | |
dc.contributor.author | Langer, JD | |
dc.contributor.author | Kruse, K | |
dc.contributor.author | Kirchner, L | |
dc.contributor.author | Sanders, K | |
dc.contributor.author | Daum, B | |
dc.contributor.author | Averhoff, B | |
dc.contributor.author | Gold, VAM | |
dc.date.accessioned | 2020-05-07T15:05:28Z | |
dc.date.issued | 2020-05-06 | |
dc.description.abstract | Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus (‘wide’ and ‘narrow’), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility. | en_GB |
dc.description.sponsorship | Biotechnology & Biological Sciences Research Council (BBSRC) | en_GB |
dc.description.sponsorship | Max-Planck-Society | en_GB |
dc.description.sponsorship | University of Exeter | en_GB |
dc.description.sponsorship | Deutsche Forschungsgemeinschaft | en_GB |
dc.identifier.citation | Vol. 11, article 2231 | en_GB |
dc.identifier.doi | 10.1038/s41467-020-15650-w | |
dc.identifier.grantnumber | BB/R008639/1 | en_GB |
dc.identifier.grantnumber | AV 9/6-2 | en_GB |
dc.identifier.uri | http://hdl.handle.net/10871/120975 | |
dc.language.iso | en | en_GB |
dc.publisher | Nature Research | en_GB |
dc.rights | © 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/. | en_GB |
dc.title | Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2020-05-07T15:05:28Z | |
exeter.article-number | 2231 | en_GB |
dc.description | This is the final version. Available on open access from Nature Research via the DOI in this record | en_GB |
dc.description | Data availability:
EM maps have been deposited in the Electron Microscopy Data Bank (EMDB, https://www.ebi.ac.uk/pdbe/emdb/) with accession codes EMD-10647 (wide pilus, PilA4) and EMD-10648 (narrow pilus, PilA5). Models have been deposited in the Protein Data Bank (PDB, https://www.rcsb.org/) with accession codes 6XXD (PilA4) and 6XXE (PilA5). The MS proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE75 partner repository (https://www.ebi.ac.uk/pride/) with dataset identifier PXD017353. The source data underlying Figs. 5c–e and 6, Supplementary Figs. 2, 3b, c, 4a–c, 5e and 6e, f, and Supplementary Table 4 are provided in the Source Data file. Uncropped versions of gels and blots (for Fig. 5c, d, and Supplementary Figs. 2b and 4a–c) and twitching images (for Fig. 6a) are also shown in Supplementary Fig. 10. | en_GB |
dc.identifier.eissn | 2041-1723 | |
dc.identifier.journal | Nature Communications | en_GB |
dc.rights.uri | http://www.rioxx.net/licenses/all-rights-reserved | en_GB |
dcterms.dateAccepted | 2020-03-19 | |
exeter.funder | ::Wellcome Trust | en_GB |
exeter.funder | ::Biotechnology & Biological Sciences Research Council (BBSRC) | en_GB |
rioxxterms.version | VoR | en_GB |
rioxxterms.licenseref.startdate | 2020-05-06 | |
rioxxterms.type | Journal Article/Review | en_GB |
refterms.dateFCD | 2020-05-07T15:02:45Z | |
refterms.versionFCD | VoR | |
refterms.dateFOA | 2020-05-07T15:05:38Z | |
refterms.panel | A | en_GB |