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PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus

Treuner-Lange, Anke and Chang, Yi-Wei and Glatter, Timo and Herfurth, Marco and Lindow, Steffi and Chreifi, Georges and Jensen, Grant J. and Søgaard-Andersen, Lotte (2020) PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus. Nature Communications, 11 . Art. No. 5054. ISSN 2041-1723.

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Type IVa pili are ubiquitous and versatile bacterial cell surface filaments that undergo cycles of extension, adhesion and retraction powered by the cell-envelope spanning type IVa pilus machine (T4aPM). The overall architecture of the T4aPM and the location of 10 conserved core proteins within this architecture have been elucidated. Here, using genetics, cell biology, proteomics and cryo-electron tomography, we demonstrate that the PilY1 protein and four minor pilins, which are widely conserved in T4aP systems, are essential for pilus extension in Myxococcus xanthus and form a complex that is an integral part of the T4aPM. Moreover, these proteins are part of the extended pilus. Our data support a model whereby the PilY1/minor pilin complex functions as a priming complex in T4aPM for pilus extension, a tip complex in the extended pilus for adhesion, and a cork for terminating retraction to maintain a priming complex for the next round of extension.

Item Type:Article
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URLURL TypeDescription
Treuner-Lange, Anke0000-0001-6435-5642
Chang, Yi-Wei0000-0003-2391-473X
Chreifi, Georges0000-0003-4194-1694
Jensen, Grant J.0000-0003-1556-4864
Søgaard-Andersen, Lotte0000-0002-0674-0013
Additional Information:© The Author(s) 2020. 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 Received 30 September 2019. Accepted 14 September 2020. Published 07 October 2020. We thank Ahmet Tekin for strains and plasmids and Magdalena Anna Świątek-Połatyńska for LonD antibodies. Cryo-ET work was done in the Beckman Institute Resource Center for Transmission Electron Microscopy at Caltech. This work was supported by the Deutsche Forschungsgemeinschaft (DFG) within the framework of the SFB987 “Microbial Diversity in Environmental Signal response” (to L.S.-A.), the Max Planck Society (to L.S.-A.), and NIH grant RO1 AI27401 (to G.J.J.). Data availability. The proteomics datasets are available via the PRIDE database (ProteomeXchange accession: PXD021163). We also used the following publicly available datasets: Uniprot ( and KEGG (, including the KEGG SSDB database ( Source data are provided with this paper. Open Access funding enabled and organized by Projekt DEAL. Author Contributions. A.T.-L.: designed and conceived the study and performed most of the experiments. Y.-W.C.: performed the cryo-electron tomographic experiments and the modeling of the priming complex. T.G.: performed purification and analysis of pull-down samples and label-free mass spectrometry-based quantitative proteomics. S.L.: generated plasmids and strains and performed motility assays. M.H.: generated plasmids and strains and helped with transmission electron microscopy and bioinformatics. G.C.: helped with cryo-electron tomography data acquisition. G.J.J. and L.S.-A.: conceived the study, supervised research and provided funding. A.T.-L., Y.-W.C., T.G., G.J.J., and L.S.-A.: analyzed and interpreted data and wrote the manuscript. All authors approved the final manuscript. The authors declare no competing interests. Reporting summary. Further information on research design is available in the Nature Research Reporting Summary linked to this article. Peer review information. Nature Communications thanks Lisa Craig and the other anonymous reviewers for their contribution to the peer review of this work. Peer reviewer reports are available.
Funding AgencyGrant Number
Deutsche Forschungsgemeinschaft (DFG)SFB987
NIHR01 AI27401
Record Number:CaltechAUTHORS:20201008-083808921
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Official Citation:Treuner-Lange, A., Chang, Y., Glatter, T. et al. PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus. Nat Commun 11, 5054 (2020).
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:105912
Deposited By: George Porter
Deposited On:08 Oct 2020 16:25
Last Modified:08 Oct 2020 16:25

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