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RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis.
Morgenstein, Randy M; Bratton, Benjamin P; Nguyen, Jeffrey P; Ouzounov, Nikolay; Shaevitz, Joshua W; Gitai, Zemer.
Afiliação
  • Morgenstein RM; Department of Molecular Biology, Princeton University, Princeton, NJ 08544;
  • Bratton BP; Department of Molecular Biology, Princeton University, Princeton, NJ 08544; Lewis-Sigler Institute for Integrative Genomics, Princeton, NJ 08544;
  • Nguyen JP; Department of Physics, Princeton University, Princeton, NJ 08544.
  • Ouzounov N; Department of Molecular Biology, Princeton University, Princeton, NJ 08544;
  • Shaevitz JW; Lewis-Sigler Institute for Integrative Genomics, Princeton, NJ 08544; Department of Physics, Princeton University, Princeton, NJ 08544.
  • Gitai Z; Department of Molecular Biology, Princeton University, Princeton, NJ 08544; zgitai@princeton.edu.
Proc Natl Acad Sci U S A ; 112(40): 12510-5, 2015 Oct 06.
Article em En | MEDLINE | ID: mdl-26396257
ABSTRACT
The rod shape of most bacteria requires the actin homolog, MreB. Whereas MreB was initially thought to statically define rod shape, recent studies found that MreB dynamically rotates around the cell circumference dependent on cell wall synthesis. However, the mechanism by which cytoplasmic MreB is linked to extracytoplasmic cell wall synthesis and the function of this linkage for morphogenesis has remained unclear. Here we demonstrate that the transmembrane protein RodZ mediates MreB rotation by directly or indirectly coupling MreB to cell wall synthesis enzymes. Furthermore, we map the RodZ domains that link MreB to cell wall synthesis and identify mreB mutants that suppress the shape defect of ΔrodZ without restoring rotation, uncoupling rotation from rod-like growth. Surprisingly, MreB rotation is dispensable for rod-like shape determination under standard laboratory conditions but is required for the robustness of rod shape and growth under conditions of cell wall stress.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Parede Celular / Proteínas de Escherichia coli / Proteínas do Citoesqueleto / Escherichia coli Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Parede Celular / Proteínas de Escherichia coli / Proteínas do Citoesqueleto / Escherichia coli Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2015 Tipo de documento: Article