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Cho H, Wivagg CN, Kapoor M, et al. Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat Microbiol. 2016;1:16172doi: 10.1038/nmicrobiol.2016.172.
Cho, H., Wivagg, C. N., Kapoor, M., Barry, Z., Rohs, P. D. A., Suh, H., Marto, J. A., Garner, E. C., & Bernhardt, T. G. (2016). Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nature microbiology, 116172. https://doi.org/10.1038/nmicrobiol.2016.172
Cho, Hongbaek, et al. "Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously." Nature microbiology vol. 1 (2016): 16172. doi: https://doi.org/10.1038/nmicrobiol.2016.172
Cho H, Wivagg CN, Kapoor M, Barry Z, Rohs PDA, Suh H, Marto JA, Garner EC, Bernhardt TG. Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat Microbiol. 2016 Sep 19;1:16172. doi: 10.1038/nmicrobiol.2016.172. PMID: 27643381; PMCID: PMC5030067.
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Nat Microbiol. 2016 Sep 19;1:16172. doi: 10.1038/nmicrobiol.2016.172.

Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously.

Nature microbiology

Hongbaek Cho, Carl N Wivagg, Mrinal Kapoor, Zachary Barry, Patricia D A Rohs, Hyunsuk Suh, Jarrod A Marto, Ethan C Garner, Thomas G Bernhardt

Affiliations

  1. Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
  2. Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
  3. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
  4. Department of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, USA.

PMID: 27643381 PMCID: PMC5030067 DOI: 10.1038/nmicrobiol.2016.172

Abstract

Multi-protein complexes organized by cytoskeletal proteins are essential for cell wall biogenesis in most bacteria. Current models of the wall assembly mechanism assume that class A penicillin-binding proteins (aPBPs), the targets of penicillin-like drugs, function as the primary cell wall polymerases within these machineries. Here, we use an in vivo cell wall polymerase assay in Escherichia coli combined with measurements of the localization dynamics of synthesis proteins to investigate this hypothesis. We find that aPBP activity is not necessary for glycan polymerization by the cell elongation machinery, as is commonly believed. Instead, our results indicate that cell wall synthesis is mediated by two distinct polymerase systems, shape, elongation, division, sporulation (SEDS)-family proteins working within the cytoskeletal machines and aPBP enzymes functioning outside these complexes. These findings thus necessitate a fundamental change in our conception of the cell wall assembly process in bacteria.

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