SEDS proteins are a widespread family of bacterial cell wall polymerases
Meeske, Alexander J.
Riley, Eammon P.
Mekelanos, John J.
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CitationMeeske, Alexander J., Eammon P. Riley, William P. Robins, Tsuyoshi Uehara, John J. Mekelanos, Daniel Kahne, Suzanne Walker, Andrew C. Kruse, Thomas G. Bernhardt, and David Z. Rudner. 2016. “SEDS proteins are a widespread family of bacterial cell wall polymerases.” Nature 537 (7622): 634-638. doi:10.1038/nature19331. http://dx.doi.org/10.1038/nature19331.
AbstractSummary Elongation of rod-shaped bacteria is mediated by a dynamic peptidoglycan synthetic machinery called the Rod complex. 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 expression of RodA, a widely conserved core component of the Rod complex. RodA is a member of the SEDS family of proteins that play 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 new family of peptidoglycan polymerases. Thus, B. subtilis and likely most bacteria use two distinct classes of polymerases 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.
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