@article{84241,
  keywords = {rotation, Mutation, Escherichia coli, Protein Binding, Luminescent Proteins, Microscopy, Fluorescence, Microscopy, Phase-Contrast, Escherichia coli Proteins, Cytoskeletal Proteins, Time-Lapse Imaging, Cell Wall},
  author = {Randy Morgenstein and Benjamin Bratton and Jeffrey Nguyen and Nikolay Ouzounov and Joshua Shaevitz and Zemer Gitai},
  title = {RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis.},
  abstract = {<p>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.</p>
},
  year = {2015},
  journal = {Proc Natl Acad Sci U S A},
  volume = {112},
  pages = {12510-5},
  month = {10/2015},
  issn = {1091-6490},
  doi = {10.1073/pnas.1509610112},
  language = {eng},
}