Structural changes of TasA in biofilm formation of Bacillus subtilis

verfasst von

Anne Diehl, Yvette Roske, Linda Ball, Anup Chowdhury, Matthias Hiller, Noel Molière, Regina Kramer, Daniel Stöppler, Catherine L. Worth, Brigitte Schlegel, Martina Leidert, Nils Cremer, Natalja Erdmann, Daniel Lopez, Heike Stephanowitz, Eberhard Krause, Barth Jan van Rossum, Peter Schmieder, Udo Heinemann, Kürşad Turgay, Ümit Akbey, Hartmut Oschkinat

Abstract

Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics. Bacillus subtilis biofilms contain TasA as major proteinaceous component in addition to exopolysaccharides. In stark contrast to the initially unfolded biofilm proteins of other bacteria, TasA is a soluble, stably folded monomer, whose structure we have determined by X-ray crystallography. Subsequently, we characterized in vitro different oligomeric forms of TasA by NMR, EM, X-ray diffraction, and analytical ultracentrifugation (AUC) experiments. However, by magic-angle spinning (MAS) NMR on live biofilms, a swift structural change toward only one of these forms, consisting of homogeneous and protease-resistant, β-sheet–rich fibrils, was observed in vivo. Thereby, we characterize a structural change from a globular state to a fibrillar form in a functional prokaryotic system on the molecular level.

Organisationseinheit(en)

Institut für Mikrobiologie

Externe Organisation(en)

Leibniz-Institut für Molekulare Pharmakologie (FMP)
Max-Delbrück-Centrum für Molekulare Medizin (MDC) in der Helmholtz-Gemeinschaft
Freie Universität Berlin (FU Berlin)
Universidad Autónoma de Madrid (UAM)
Aarhus University

Typ

Artikel

Journal

Proceedings of the National Academy of Sciences of the United States of America

Band

115

Seiten

3237-3242

Anzahl der Seiten

6

ISSN

0027-8424

Publikationsdatum

27.03.2018

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Allgemein

Elektronische Version(en)

https://doi.org/10.1073/pnas.1718102115 (Zugang: Offen)
https://doi.org/10.15488/3384 (Zugang: Offen)