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Structural changes of TasA in biofilm formation of Bacillus subtilis.

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Diehl A, Roske Y, Ball L, Chowdhury A, Hiller M, Moli猫re N, Kramer R, St枚ppler D, Worth CL, Schlegel B, Leidert M, Cremer N, Erdmann N, Lopez D, Stephanowitz H, Krause E, van Rossum BJ, Schmieder P, Heinemann U, Turgay K, Akbey 脺, Oschkinat H
OpenAccess logo Proc Natl Acad Sci U S A 115 3237-3242 (2018)
Cited: 55 times
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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, 尾-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.

Reviews - 5of1 mentioned but not cited (1)

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Articles - 5of1 mentioned but not cited (8)

  1. Diehl A, Roske Y, Ball L, Chowdhury A, Hiller M, Moli猫re N, Kramer R, St枚ppler D, Worth CL, Schlegel B, Leidert M, Cremer N, Erdmann N, Lopez D, Stephanowitz H, Krause E, van Rossum BJ, Schmieder P, Heinemann U, Turgay K, Akbey 脺, Oschkinat H. Proc Natl Acad Sci U S A 115 3237-3242 (2018)
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Reviews citing this publication (17)

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