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

  • 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.
Author:Alexander Neuhaus, Muniyandi Selvaraj, Ralf SalzerORCiDGND, Julian David LangerORCiDGND, Kerstin KruseGND, Lennart Kirchner, Kelly Sanders, Bertram Daum, Beate AverhoffORCiD, Vicki A. M. GoldORCiD
Parent Title (English):Nature Communications
Publisher:Nature Publishing Group UK
Place of publication:[London]
Document Type:Article
Year of Completion:2020
Date of first Publication:2020/05/06
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2020/05/11
Tag:Bacterial structural biology; Cellular microbiology; Cryoelectron microscopy
Issue:1, Art. 2231
Page Number:13
First Page:1
Last Page:13
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Institutes:Biowissenschaften / Biowissenschaften
Angeschlossene und kooperierende Institutionen / MPI für Biophysik
Angeschlossene und kooperierende Institutionen / MPI für Hirnforschung
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0