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

Alexander Neuhaus, Muniyandi Selvaraj, Ralf Salzer, Julian D. Langer, Kerstin Kruse, Lennart Kirchner, Kelly Sanders, Bertram Daum, Beate Averhoff and Vicki A. M. Gold ()
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Alexander Neuhaus: Living Systems Institute, University of Exeter, Stocker Road
Muniyandi Selvaraj: Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3
Ralf Salzer: Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue Str. 9
Julian D. Langer: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3
Kerstin Kruse: Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue Str. 9
Lennart Kirchner: Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue Str. 9
Kelly Sanders: Living Systems Institute, University of Exeter, Stocker Road
Bertram Daum: Living Systems Institute, University of Exeter, Stocker Road
Beate Averhoff: Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue Str. 9
Vicki A. M. Gold: Living Systems Institute, University of Exeter, Stocker Road

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-15650-w

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