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The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation

Author

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  • Sebastian A. G. Braus

    (Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5)

  • Francesca L. Short

    (Monash University)

  • Stefanie Holz

    (Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5)

  • Matthew J. M. Stedman

    (Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5)

  • Alvar D. Gossert

    (Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5)

  • Manuela K. Hospenthal

    (Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5)

Abstract

Naturally competent bacteria encode sophisticated protein machinery for the uptake and translocation of exogenous DNA into the cell. If this DNA is integrated into the bacterial genome, the bacterium is said to be naturally transformed. Most competent bacterial species utilise type IV pili for the initial DNA uptake step. These proteinaceous cell-surface structures are composed of thousands of pilus subunits (pilins), designated as major or minor according to their relative abundance in the pilus. Here, we show that the minor pilin FimT plays an important role in the natural transformation of Legionella pneumophila. We use NMR spectroscopy, in vitro DNA binding assays and in vivo transformation assays to understand the molecular basis of FimT’s role in this process. FimT binds to DNA via an electropositive patch, rich in arginines, several of which are well-conserved and located in a conformationally flexible C-terminal tail. FimT orthologues from other Gammaproteobacteria share the ability to bind to DNA. Our results suggest that FimT plays an important role in DNA uptake in a wide range of competent species.

Suggested Citation

  • Sebastian A. G. Braus & Francesca L. Short & Stefanie Holz & Matthew J. M. Stedman & Alvar D. Gossert & Manuela K. Hospenthal, 2022. "The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28690-1
    DOI: 10.1038/s41467-022-28690-1
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    References listed on IDEAS

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    1. Alexander Neuhaus & Muniyandi Selvaraj & Ralf Salzer & Julian D. Langer & Kerstin Kruse & Lennart Kirchner & Kelly Sanders & Bertram Daum & Beate Averhoff & Vicki A. M. Gold, 2020. "Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    2. Sara J. Weaver & Davi R. Ortega & Matthew H. Sazinsky & Triana N. Dalia & Ankur B. Dalia & Grant J. Jensen, 2020. "Publisher Correction: CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholera," Nature Communications, Nature, vol. 11(1), pages 1-1, December.
    3. Anke Treuner-Lange & Yi-Wei Chang & Timo Glatter & Marco Herfurth & Steffi Lindow & Georges Chreifi & Grant J. Jensen & Lotte Søgaard-Andersen, 2020. "PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    4. Sara J. Weaver & Davi R. Ortega & Matthew H. Sazinsky & Triana N. Dalia & Ankur B. Dalia & Grant J. Jensen, 2020. "CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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