The lipid II flippase RodA determines morphology and growth in Corynebacterium glutamicum

Mol Microbiol. 2013 Dec;90(5):966-82. doi: 10.1111/mmi.12411. Epub 2013 Oct 22.

Abstract

Lipid II flippases play an essential role in cell growth and the maintenance of cell shape in many rod-shaped bacteria. The putative lipid II flippase RodA is an integral membrane protein and member of the SEDS (shape, elongation, division and sporulation) protein family. In contrast to its homologues in Escherichia coli and Bacillus subtilis little is known about the role of RodA in actinobacteria. In this study, we describe the localization and function of RodA in Corynebacterium glutamicum, a rod-shaped, apically growing actinobacterium. RodA-GFP localizes exclusively at the cell poles. Surprisingly, time-lapse microscopy revealed that apical cell growth is sustained in a rodA deletion strain. However, growth rates and antibiotic susceptibility are altered. In the absence of RodA, it appears that apical growth is driven by lateral diffusion of lipid II that is likely flipped by the septal flippase, FtsW. Furthermore, we applied a previously described synthetic in vivo system in combination with FRET to identify an interaction between C. glutamicum RodA and the polar growth organizing protein DivIVA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / metabolism*
  • Cell Cycle Proteins / metabolism
  • Cell Division
  • Cell Wall / metabolism
  • Corynebacterium glutamicum / cytology*
  • Corynebacterium glutamicum / enzymology
  • Corynebacterium glutamicum / growth & development*
  • Fluorescence Resonance Energy Transfer
  • Gene Deletion
  • Membrane Proteins / metabolism*
  • Nisin / pharmacology
  • Time-Lapse Imaging
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives*
  • Uridine Diphosphate N-Acetylmuramic Acid / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Cell Cycle Proteins
  • DivIVA protein, bacteria
  • Membrane Proteins
  • Uridine Diphosphate N-Acetylmuramic Acid
  • muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol
  • FtsW protein, Bacteria
  • Nisin