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Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall

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  • Huan Zhang

    (Texas A&M University)

  • Srutha Venkatesan

    (Texas A&M University)

  • Emily Ng

    (Texas A&M University)

  • Beiyan Nan

    (Texas A&M University)

Abstract

Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates the distribution and dynamics of aPBPs. Our findings clarify the action of moenomycin and suggest that disrupting the coordination between PG synthases and hydrolases could be more lethal than eliminating individual enzymes.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41082-3
    DOI: 10.1038/s41467-023-41082-3
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    References listed on IDEAS

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    1. Timothy K. Lee & Kevin Meng & Handuo Shi & Kerwyn Casey Huang, 2016. "Single-molecule imaging reveals modulation of cell wall synthesis dynamics in live bacterial cells," Nature Communications, Nature, vol. 7(1), pages 1-9, December.
    2. 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.
    3. Ling Juan Wu & Seoungjun Lee & Sungshic Park & Lucy E. Eland & Anil Wipat & Séamus Holden & Jeff Errington, 2020. "Geometric principles underlying the proliferation of a model cell system," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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