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| Item Type: | Article |
|---|---|
| Title: | Structural changes of TasA in biofilm formation of Bacillus subtilis |
| Creators Name: | Diehl, A. and Roske, Y. and Ball, L. and Chowdhury, A. and Hiller, M. and Molière, N. and Kramer, R. and Stöppler, D. and Worth, C.L. and Schlegel, B. and Leidert, M. and Cremer, N. and Erdmann, N. and Lopez, D. and Stephanowitz, H. and Krause, E. and van Rossum, B.J. and Schmieder, P. and Heinemann, U. and Turgay, K. and Akbey, Ü. and Oschkinat, H. |
| 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. |
| Keywords: | Biofilm, TasA, Bacillus subtilis, Structure, NMR |
| Source: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Volume: | 115 |
| Number: | 13 |
| Page Range: | 3237-3242 |
| Date: | 27 March 2018 |
| Official Publication: | https://doi.org/10.1073/pnas.1718102115 |
| PubMed: | View item in PubMed |
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