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The molecular basis of regulation of bacterial capsule assembly by Wzc

Author

Listed:
  • Yun Yang

    (Rosalind Franklin Institute, Harwell Campus
    The University of Oxford
    The Research Complex at Harwell, Harwell Campus)

  • Jiwei Liu

    (Rosalind Franklin Institute, Harwell Campus
    The University of Oxford)

  • Bradley R. Clarke

    (The University of Guelph)

  • Laura Seidel

    (The University of Guelph)

  • Jani R. Bolla

    (The University of Oxford
    The Kavli Institute for Nanoscience Discovery)

  • Philip N. Ward

    (Rosalind Franklin Institute, Harwell Campus
    The University of Oxford
    The Research Complex at Harwell, Harwell Campus)

  • Peijun Zhang

    (The University of Oxford
    Harwell Science and Innovation Campus)

  • Carol V. Robinson

    (The University of Oxford
    The Kavli Institute for Nanoscience Discovery)

  • Chris Whitfield

    (The University of Guelph)

  • James H. Naismith

    (Rosalind Franklin Institute, Harwell Campus
    The University of Oxford
    The Research Complex at Harwell, Harwell Campus)

Abstract

Bacterial extracellular polysaccharides (EPSs) play critical roles in virulence. Many bacteria assemble EPSs via a multi-protein “Wzx-Wzy” system, involving glycan polymerization at the outer face of the cytoplasmic/inner membrane. Gram-negative species couple polymerization with translocation across the periplasm and outer membrane and the master regulator of the system is the tyrosine autokinase, Wzc. This near atomic cryo-EM structure of dephosphorylated Wzc from E. coli shows an octameric assembly with a large central cavity formed by transmembrane helices. The tyrosine autokinase domain forms the cytoplasm region, while the periplasmic region contains small folded motifs and helical bundles. The helical bundles are essential for function, most likely through interaction with the outer membrane translocon, Wza. Autophosphorylation of the tyrosine-rich C-terminus of Wzc results in disassembly of the octamer into multiply phosphorylated monomers. We propose that the cycling between phosphorylated monomer and dephosphorylated octamer regulates glycan polymerization and translocation.

Suggested Citation

  • Yun Yang & Jiwei Liu & Bradley R. Clarke & Laura Seidel & Jani R. Bolla & Philip N. Ward & Peijun Zhang & Carol V. Robinson & Chris Whitfield & James H. Naismith, 2021. "The molecular basis of regulation of bacterial capsule assembly by Wzc," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24652-1
    DOI: 10.1038/s41467-021-24652-1
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    Cited by:

    1. Amandine Nucci & Eduardo P. C. Rocha & Olaya Rendueles, 2022. "Adaptation to novel spatially-structured environments is driven by the capsule and alters virulence-associated traits," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Jinsheng Tang & Mengru Guo & Min Chen & Bin Xu & Tingting Ran & Weiwu Wang & Zhe Ma & Huixing Lin & Hongjie Fan, 2023. "A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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