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PilY1 and minor pilins form a complex priming the type IVa pilus in Myxococcus xanthus

Author

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  • Anke Treuner-Lange

    (Max Planck Institute for Terrestrial Microbiology)

  • Yi-Wei Chang

    (California Institute of Technology
    University of Pennsylvania)

  • Timo Glatter

    (Max Planck Institute for Terrestrial Microbiology)

  • Marco Herfurth

    (Max Planck Institute for Terrestrial Microbiology)

  • Steffi Lindow

    (Max Planck Institute for Terrestrial Microbiology)

  • Georges Chreifi

    (California Institute of Technology)

  • Grant J. Jensen

    (California Institute of Technology
    California Institute of Technology)

  • Lotte Søgaard-Andersen

    (Max Planck Institute for Terrestrial Microbiology)

Abstract

Type IVa pili are ubiquitous and versatile bacterial cell surface filaments that undergo cycles of extension, adhesion and retraction powered by the cell-envelope spanning type IVa pilus machine (T4aPM). The overall architecture of the T4aPM and the location of 10 conserved core proteins within this architecture have been elucidated. Here, using genetics, cell biology, proteomics and cryo-electron tomography, we demonstrate that the PilY1 protein and four minor pilins, which are widely conserved in T4aP systems, are essential for pilus extension in Myxococcus xanthus and form a complex that is an integral part of the T4aPM. Moreover, these proteins are part of the extended pilus. Our data support a model whereby the PilY1/minor pilin complex functions as a priming complex in T4aPM for pilus extension, a tip complex in the extended pilus for adhesion, and a cork for terminating retraction to maintain a priming complex for the next round of extension.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18803-z
    DOI: 10.1038/s41467-020-18803-z
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    Cited by:

    1. Saima Rehman & Anna Katarina Antonovic & Ian E. McIntire & Huaixin Zheng & Leanne Cleaver & Maria Baczynska & Carlton O. Adams & Theo Portlock & Katherine Richardson & Rosie Shaw & Alain Oregioni & Gi, 2024. "The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Liuyang Li & Danyue Huang & Yaoxun Hu & Nicola M. Rudling & Daniel P. Canniffe & Fengping Wang & Yinzhao Wang, 2023. "Globally distributed Myxococcota with photosynthesis gene clusters illuminate the origin and evolution of a potentially chimeric lifestyle," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. 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.
    4. Robin Anger & Laetitia Pieulle & Meriam Shahin & Odile Valette & Hugo Guenno & Artemis Kosta & Vladimir Pelicic & Rémi Fronzes, 2023. "Structure of a heteropolymeric type 4 pilus from a monoderm bacterium," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    5. María Pérez-Burgos & Marco Herfurth & Andreas Kaczmarczyk & Andrea Harms & Katrin Huber & Urs Jenal & Timo Glatter & Lotte Søgaard-Andersen, 2024. "A deterministic, c-di-GMP-dependent program ensures the generation of phenotypically similar, symmetric daughter cells during cytokinesis," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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