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

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

Authors: Alexander Neuhaus (University of Exeter) , Muniyandi Selvaraj (University of Helsinki; Max Planck Institute of Biophysics) , Ralf Salzer (Medical Research Council—Laboratory of Molecular Biology; Goethe University Frankfurt) , Julian D. Langer (Max Planck Institute of Biophysics) , Kerstin Kruse (Goethe University Frankfurt) , Lennart Kirchner (Goethe University Frankfurt) , Kelly Sanders (University of Exeter) , Bertram Daum (University of Exeter) , Beate Averhoff (Goethe University Frankfurt) , Vicki A. M. Gold (University of Exeter)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 11

State: Published (Approved)
Published: May 2020
Diamond Proposal Number(s): 18258

Open Access Open Access

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.

Journal Keywords: Bacterial structural biology; Cellular microbiology; Cryoelectron microscopy

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios II-Titan Krios II at Diamond

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s41467-020-15650-w.pdf