English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Other

Structural changes of TasA in biofilm formation of Bacillus subtilis

MPS-Authors
/persons/resource/persons47565

Akbey,  Ümit
MPI for Polymer Research, Max Planck Society;
FMP Leibniz Inst Mol Pharmakol, NMR Supported Struct Biol, D-13125 Berlin, Germany;

/persons/resource/persons78477

Oschkinat,  Hartmut
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Diehl, A., Roske, Y., Ball, L., Chowdhury, A., Hiller, M., Molière, N., et al. (2018). Structural changes of TasA in biofilm formation of Bacillus subtilis.


Cite as: http://hdl.handle.net/21.11116/0000-0008-7D2E-A
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.