Structural changes of TasA in biofilm formation of Bacillus subtilis

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

DOI

  • Anne Diehl, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Yvette Roske, Max Delbruck Ctr Mol Med, Helmholtz Association, Max Delbruck Center for Molecular Medicine
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  • Linda Ball, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Anup Chowdhury, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Matthias Hiller, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Noel Moliere, Leibniz Univ Hannover, University of Hannover, Inst Mikrobiol
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  • Regina Kramer, Leibniz Univ Hannover, University of Hannover, Inst Mikrobiol
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  • Daniel Stoeppler, Free Univ Berlin, Free University of Berlin, Inst Chem & Biochem
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  • Catherine L. Worth, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Brigitte Schlegel, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Martina Leidert, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Nils Cremer, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Natalja Erdmann, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Daniel Lopez, Univ Autonoma Madrid, Autonomous University of Madrid, Consejo Superior de Investigaciones Cientificas (CSIC), CSIC - Centro Nacional de Biotecnologia (CNB), Ctr Nacl Biotecnol
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  • Heike Stephanowitz, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Eberhard Krause, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Barth-Jan van Rossum, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Peter Schmieder, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Udo Heinemann, Free Univ Berlin, Free University of Berlin, Inst Chem & Biochem
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  • Kursad Turgay, Leibniz Univ Hannover, University of Hannover, Inst Mikrobiol
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  • Umit Akbey, Leibniz Forschungsinst Mol Pharmakol, Leibniz Forschungsinstitut furr Molekulare Pharmakologie (FMP)
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  • Hartmut Oschkinat, Free Univ Berlin, Free University of Berlin, Inst Chem & Biochem

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.

Original languageEnglish
JournalProceedings of the National Academy of Sciences of the United States of America
Volume115
Issue13
Pages (from-to)3237-3242
Number of pages6
ISSN0027-8424
DOIs
Publication statusPublished - 27 Mar 2018

    Research areas

  • biofilm, TasA, Bacillus subtilis, structure, NMR, POLYPROLINE-II HELIX, SIGNAL PEPTIDASE, MASTER REGULATOR, AMYLOID FIBERS, PROTEIN, IDENTIFICATION, MATRIX, SURFACE, CEREUS, MECHANISMS, Molecular Weight, Crystallography, X-Ray, Metalloendopeptidases/chemistry, Biofilms/growth & development, Ultracentrifugation, Bacterial Proteins/chemistry, Magnetic Resonance Spectroscopy, Bacillus subtilis/chemistry, Models, Molecular, Microscopy, Electron, Calorimetry, Protein Conformation, Structural Homology, Protein, Hydrogen-Ion Concentration

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