SEDS proteins are a widespread family of bacterial cell wall polymerases

Alexander J. Meeske, Eammon P. Riley, William P. Robins, Tsuyoshi Uehara, John J. Mekalanos, Daniel Kahne, Suzanne Walker, Andrew C. Kruse, Thomas G. Bernhardt () and David Z. Rudner ()
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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
Suzanne Walker: Harvard Medical School
Andrew C. Kruse: Harvard Medical School
Thomas G. Bernhardt: Harvard Medical School
David Z. Rudner: Harvard Medical School

Nature, 2016, vol. 537, issue 7622, 634-638

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature19331

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