Cryo-electron microscopy reveals two distinct type IV pili assembled by the 
same bacterium

Neuhaus, Alexander; Selvaraj, Muniyandi; Salzer, Ralf; Langer, Julian David; Kruse, Kerstin; Kirchner, Lennart; Sanders, Kelly; Daum, Bertram; Averhoff, Beate; Gold, Vicky

doi:10.1038/s41467-020-15650-w

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Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium

Neuhaus, A., Selvaraj, M., Salzer, R., Langer, J. D., Kruse, K., Kirchner, L., et al. (2020). Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nature Communications, 11: 2231. doi:10.1038/s41467-020-15650-w.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0006-73DF-E Version Permalink: https://hdl.handle.net/21.11116/0000-0007-79B0-A

Genre: Journal Article

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Neuhaus, Alexander^{1, 2}, Author
Selvaraj, Muniyandi³, Author
Salzer, Ralf⁴, Author
Langer, Julian David^{5, 6, 7}, Author
Kruse, Kerstin⁴, Author
Kirchner, Lennart⁴, Author
Sanders, Kelly^{1, 2}, Author
Daum, Bertram^{1, 2}, Author
Averhoff, Beate⁴, Author
Gold, Vicky^{1, 2}, Author

Affiliations:
1Living Systems Institute, University of Exeter, UK, Stocker Road, Exeter EX4 4QD, UK, ou_persistent22
2College of Life and Environmental Sciences, Geoffrey Pope, University of Exeter, UK, Stocker Road, Exeter EX4 4QD, UK, ou_persistent22
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291
4Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Germany, Max-von-Laue Str. 9, 60438 Frankfurt am Main, Germany, ou_persistent22
5Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290
6Proteomics, Max Planck Institute for Brain Research, Frankfurt, Germany, Max-von-Laue Str. 4, 60438 Frankfurt am Main, Germany, ou_persistent22
7Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society, ou_3262216

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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.

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Language(s): eng - English

Dates: Submitted: 2019-09-11Accepted: 2020-03-19Published Online: 2020-05-06

Publication Status: Published online

Pages: 13

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Rev. Type: Peer

Identifiers: DOI: 10.1038/s41467-020-15650-w

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Title: Nature Communications

Abbreviation : Nat. Commun.

Source Genre: Journal

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Publ. Info: London : Nature Publishing Group

Pages: - Volume / Issue: 11 Sequence Number: 2231 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723