Structural changes of TasA in biofilm formation of
| Autor: | 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 |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Protein Conformation Metalloendopeptidases macromolecular substances biochemical phenomena metabolism and nutrition Calorimetry Hydrogen-Ion Concentration Biological Sciences Crystallography X-Ray Microbiology biofilm NMR Molecular Weight Microscopy Electron Biophysics and Computational Biology Bacterial Proteins Structural Homology Protein Biofilms Physical Sciences structure Ultracentrifugation TasA Bacillus subtilis |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 1091-6490 |
| Popis: | Significance Understanding the formation and structure of protective bacterial biofilms will help to design and identify antimicrobial strategies. Our experiments with the secreted major biofilm protein TasA characterize on a molecular level in vivo the transition of a folded protein into protease-resistant biofilm-stabilizing fibrils. Such conformational changes from a globular state into fibrillar structures are so far not seen for other biofilm-forming proteins. In this context, TasA can serve as a model system to study functional fibril formation from a globular state. 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. |
| Databáze: | OpenAIRE |
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