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Self-association of MreC as a regulatory signal in bacterial cell wall elongation

Author

Listed:
  • Alexandre Martins

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Carlos Contreras-Martel

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Manon Janet-Maitre

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
    Univ. Grenoble Alpes, CNRS ERL5261, CEA-IRIG-BCI, INSERM UMR1036)

  • Mayara M. Miyachiro

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Leandro F. Estrozi

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Daniel Maragno Trindade

    (Brazilian Biosciences National Laboratory (LNBio), CNPEM)

  • Caíque C. Malospirito

    (Brazilian Biosciences National Laboratory (LNBio), CNPEM
    Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP))

  • Fernanda Rodrigues-Costa

    (Brazilian Biosciences National Laboratory (LNBio), CNPEM
    Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP))

  • Lionel Imbert

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Viviana Job

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
    Univ. Grenoble Alpes, CNRS ERL5261, CEA-IRIG-BCI, INSERM UMR1036)

  • Guy Schoehn

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS))

  • Ina Attrée

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
    Univ. Grenoble Alpes, CNRS ERL5261, CEA-IRIG-BCI, INSERM UMR1036)

  • Andréa Dessen

    (Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
    Brazilian Biosciences National Laboratory (LNBio), CNPEM)

Abstract

The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be dependent on MreC self-association. Here, we use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC from Pseudomonas aeruginosa in atomic detail. MreC monomers interact in head-to-tail fashion. Longitudinal and lateral interfaces are essential for oligomerization in vitro, and a phylogenetic analysis of proteobacterial MreC sequences indicates the prevalence of the identified interfaces. Our results are consistent with a model where MreC’s ability to alternate between self-association and interaction with the cell wall biosynthesis machinery plays a key role in the regulation of elongasome activity.

Suggested Citation

  • Alexandre Martins & Carlos Contreras-Martel & Manon Janet-Maitre & Mayara M. Miyachiro & Leandro F. Estrozi & Daniel Maragno Trindade & Caíque C. Malospirito & Fernanda Rodrigues-Costa & Lionel Imbert, 2021. "Self-association of MreC as a regulatory signal in bacterial cell wall elongation," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22957-9
    DOI: 10.1038/s41467-021-22957-9
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    Cited by:

    1. 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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