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

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Selvaraj,  Muniyandi
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Proteomics, Max Planck Institute for Brain Research, Frankfurt, Germany;
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0006-73DF-E
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.