The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus

Mol Microbiol. 2007 May;64(4):938-52. doi: 10.1111/j.1365-2958.2007.05720.x.

Abstract

The tubulin homologue FtsZ is well known for its essential function in bacterial cell division. Here, we show that in Caulobacter crescentus, FtsZ also plays a major role in cell elongation by spatially regulating the location of MurG, which produces the essential lipid II peptidoglycan cell wall precursor. The early assembly of FtsZ into a highly mobile ring-like structure during cell elongation is quickly followed by the recruitment of MurG and a major redirection of peptidoglycan precursor synthesis to the midcell region. These FtsZ-dependent events occur well before cell constriction and contribute to cell elongation. In the absence of FtsZ, MurG fails to accumulate near midcell and cell elongation proceeds unperturbed in appearance by insertion of peptidoglycan material along the entire sidewalls. Evidence suggests that bacteria use both a FtsZ-independent and a FtsZ-dependent mode of peptidoglycan synthesis to elongate, the importance of each mode depending on the timing of FtsZ assembly during elongation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / analysis
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism*
  • Caulobacter crescentus / cytology
  • Caulobacter crescentus / growth & development*
  • Caulobacter crescentus / metabolism
  • Cell Wall / chemistry
  • Cell Wall / metabolism*
  • Cytoskeletal Proteins / analysis
  • Cytoskeletal Proteins / metabolism*
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • N-Acetylglucosaminyltransferases / analysis
  • N-Acetylglucosaminyltransferases / metabolism*
  • Silver Staining
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives*
  • Uridine Diphosphate N-Acetylmuramic Acid / biosynthesis

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Uridine Diphosphate N-Acetylmuramic Acid
  • muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol
  • N-Acetylglucosaminyltransferases
  • UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase