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Structural changes of TasA in biofilm formation of Bacillus subtilis

Authors

  • A. Diehl
  • Y. Roske
  • L. Ball
  • A. Chowdhury
  • M. Hiller
  • N. Molière
  • R. Kramer
  • D. Stöppler
  • C.L. Worth
  • B. Schlegel
  • M. Leidert
  • N. Cremer
  • N. Erdmann
  • D. Lopez
  • H. Stephanowitz
  • E. Krause
  • B.J. van Rossum
  • P. Schmieder
  • U. Heinemann
  • K. Turgay
  • Ü. Akbey
  • H. Oschkinat

Journal

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

Citation

  • Proc Natl Acad Sci U S A 115 (13): 3237-3242

Abstract

  • Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics.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.


DOI

doi:10.1073/pnas.1718102115