IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-10650-x.html
   My bibliography  Save this article

Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly

Author

Listed:
  • Colin J. Comerci

    (Stanford University
    Stanford University)

  • Jonathan Herrmann

    (Stanford University
    SLAC National Accelerator Laboratory)

  • Joshua Yoon

    (Stanford University
    Stanford University)

  • Fatemeh Jabbarpour

    (Stanford University
    SLAC National Accelerator Laboratory)

  • Xiaofeng Zhou

    (Stanford University)

  • John F. Nomellini

    (University of British Columbia)

  • John Smit

    (University of British Columbia)

  • Lucy Shapiro

    (Stanford University)

  • Soichi Wakatsuki

    (Stanford University
    SLAC National Accelerator Laboratory)

  • W. E. Moerner

    (Stanford University
    Stanford University
    Stanford University)

Abstract

Many bacteria and most archaea possess a crystalline protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer protein (SLP) from C. crescentus, we show that 2D protein self-assembly is sufficient to build and maintain the S-layer in living cells by efficient protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials.

Suggested Citation

  • Colin J. Comerci & Jonathan Herrmann & Joshua Yoon & Fatemeh Jabbarpour & Xiaofeng Zhou & John F. Nomellini & John Smit & Lucy Shapiro & Soichi Wakatsuki & W. E. Moerner, 2019. "Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10650-x
    DOI: 10.1038/s41467-019-10650-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-10650-x
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-019-10650-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Matthew Herdman & Buse Isbilir & Andriko Kügelgen & Ulrike Schulze & Alan Wainman & Tanmay A. M. Bharat, 2024. "Cell cycle dependent coordination of surface layer biogenesis in Caulobacter crescentus," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10650-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.