TY - JOUR

T1 - Structural changes of TasA in biofilm formation of Bacillus subtilis

AU - Diehl, Anne

AU - Roske, Yvette

AU - Ball, Linda

AU - Chowdhury, Anup

AU - Hiller, Matthias

AU - Molière, Noel

AU - Kramer, Regina

AU - Stöppler, Daniel

AU - Worth, Catherine L.

AU - Schlegel, Brigitte

AU - Leidert, Martina

AU - Cremer, Nils

AU - Erdmann, Natalja

AU - Lopez, Daniel

AU - Stephanowitz, Heike

AU - Krause, Eberhard

AU - van Rossum, Barth Jan

AU - Schmieder, Peter

AU - Heinemann, Udo

AU - Turgay, Kürşad

AU - Akbey, Ümit

AU - Oschkinat, Hartmut

N1 - Funding information: ACKNOWLEDGMENTS. We thank the team of D. Puchkov [Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP)] for electron microscopic investigations. We thank S. Runde and P. Ehrentraut (Freie Universität Berlin) for initial experiments and A. Wallmann (FMP) for making figures. This work was supported from a Joint Research Activity in the European Union Project iNext (Infrastructure for NMR, EM and X-rays for Translational Research; GA 653706) and Deutsche Forschungsgemeinschaft (Sonderforschungs-bereich 740, OS106/9, Tu106/6, and Tu106/7).

PY - 2018/3/27

Y1 - 2018/3/27

N2 - 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.

AB - 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.

KW - Bacillus subtilis

KW - Biofilm

KW - NMR

KW - Structure

KW - TasA

UR - http://www.scopus.com/inward/record.url?scp=85044421591&partnerID=8YFLogxK

U2 - 10.1073/pnas.1718102115

DO - 10.1073/pnas.1718102115

M3 - Article

C2 - 29531041

AN - SCOPUS:85044421591

VL - 115

SP - 3237

EP - 3242

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 13

ER -