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SEDS proteins are a widespread family of bacterial cell wall polymerases

Author

Listed:
  • Alexander J. Meeske

    (Harvard Medical School)

  • Eammon P. Riley

    (Harvard Medical School)

  • William P. Robins

    (Harvard Medical School)

  • Tsuyoshi Uehara

    (Harvard Medical School)

  • John J. Mekalanos

    (Harvard Medical School)

  • Daniel Kahne

    (Harvard Medical School
    Harvard University)

  • Suzanne Walker

    (Harvard Medical School
    Harvard Medical School
    Harvard University)

  • Andrew C. Kruse

    (Harvard Medical School)

  • Thomas G. Bernhardt

    (Harvard Medical School)

  • David Z. Rudner

    (Harvard Medical School)

Abstract

Elongation of rod-shaped bacteria is mediated by a dynamic peptidoglycan-synthetizing machinery called the Rod complex. Here we report that, in Bacillus subtilis, this complex is functional in the absence of all known peptidoglycan polymerases. Cells lacking these enzymes survive by inducing an envelope stress response that increases the expression of RodA, a widely conserved core component of the Rod complex. RodA is a member of the SEDS (shape, elongation, division and sporulation) family of proteins, which have essential but ill-defined roles in cell wall biogenesis during growth, division and sporulation. Our genetic and biochemical analyses indicate that SEDS proteins constitute a family of peptidoglycan polymerases. Thus, B. subtilis and probably most bacteria use two distinct classes of polymerase to synthesize their exoskeleton. Our findings indicate that SEDS family proteins are core cell wall synthases of the cell elongation and division machinery, and represent attractive targets for antibiotic development.

Suggested Citation

  • Alexander J. Meeske & Eammon P. Riley & William P. Robins & Tsuyoshi Uehara & John J. Mekalanos & Daniel Kahne & Suzanne Walker & Andrew C. Kruse & Thomas G. Bernhardt & David Z. Rudner, 2016. "SEDS proteins are a widespread family of bacterial cell wall polymerases," Nature, Nature, vol. 537(7622), pages 634-638, September.
    • Handle: RePEc:nat:nature:v:537:y:2016:i:7622:d:10.1038_nature19331
    DOI: 10.1038/nature19331
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    Cited by:

    1. Irina Shlosman & Elayne M. Fivenson & Morgan S. A. Gilman & Tyler A. Sisley & Suzanne Walker & Thomas G. Bernhardt & Andrew C. Kruse & Joseph J. Loparo, 2023. "Allosteric activation of cell wall synthesis during bacterial growth," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Yoshikazu Kawai & Maki Kawai & Eilidh Sohini Mackenzie & Yousef Dashti & Bernhard Kepplinger & Kevin John Waldron & Jeff Errington, 2023. "On the mechanisms of lysis triggered by perturbations of bacterial cell wall biosynthesis," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Michael D. Sacco & Shaohui Wang & Swamy R. Adapa & Xiujun Zhang & Eric M. Lewandowski & Maura V. Gongora & Dimitra Keramisanou & Zachary D. Atlas & Julia A. Townsend & Jean R. Gatdula & Ryan T. Morgan, 2022. "A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    4. Huan Zhang & Srutha Venkatesan & Emily Ng & Beiyan Nan, 2023. "Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    5. Shailab Shrestha & Najwa Taib & Simonetta Gribaldo & Aimee Shen, 2023. "Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    6. Rie Nygaard & Chris L. B. Graham & Meagan Belcher Dufrisne & Jonathan D. Colburn & Joseph Pepe & Molly A. Hydorn & Silvia Corradi & Chelsea M. Brown & Khuram U. Ashraf & Owen N. Vickery & Nicholas S. , 2023. "Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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