FtsW activity and lipid II synthesis are required for recruitment of MurJ to midcell during cell division in Escherichia coli

Mol Microbiol. 2018 Sep;109(6):855-884. doi: 10.1111/mmi.14104. Epub 2018 Sep 26.

Abstract

Peptidoglycan (PG) is the unique cell shape-determining component of the bacterial envelope, and is a key target for antibiotics. PG synthesis requires the transmembrane movement of the precursor lipid II, and MurJ has been shown to provide this activity in Escherichia coli. However, how MurJ functions in vivo has not been reported. Here we show that MurJ localizes both in the lateral membrane and at midcell, and is recruited to midcell simultaneously with late-localizing divisome proteins and proteins MraY and MurG. MurJ septal localization is dependent on the presence of a complete and active divisome, lipid II synthesis and PBP3/FtsW activities. Inactivation of MurJ, either directly by mutation or through binding with MTSES, did not affect the midcell localization of MurJ. Our study visualizes MurJ localization in vivo and reveals a possible mechanism of MurJ recruitment during cell division.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Cell Division / genetics*
  • Cell Wall / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism
  • Membrane Proteins / genetics*
  • Mesylates / pharmacology
  • Peptidoglycan / metabolism
  • Phospholipid Transfer Proteins / genetics*
  • Phospholipid Transfer Proteins / metabolism
  • Transferases (Other Substituted Phosphate Groups)
  • Transferases / metabolism
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives*
  • Uridine Diphosphate N-Acetylmuramic Acid / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Mesylates
  • MurJ protein, E coli
  • Peptidoglycan
  • Phospholipid Transfer Proteins
  • Uridine Diphosphate N-Acetylmuramic Acid
  • muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol
  • FtsW protein, Bacteria
  • (2-sulfonatoethyl)methanethiosulfonate
  • Transferases
  • Transferases (Other Substituted Phosphate Groups)
  • mraY protein, Bacteria