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Science. 2014 Jul 11;345(6193):220-2. doi: 10.1126/science.1254522.

Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis.

Author information

  • 1Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
  • 2Department of Microbiology, Ohio State University, Columbus, OH 43210, USA.
  • 3Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
  • 4Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
  • 5Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA. thomas_bernhardt@hms.harvard.edu ruiz.82@osu.edu.
  • 6Department of Microbiology, Ohio State University, Columbus, OH 43210, USA. thomas_bernhardt@hms.harvard.edu ruiz.82@osu.edu.

Abstract

Peptidoglycan (PG) is a polysaccharide matrix that protects bacteria from osmotic lysis. Inhibition of its biogenesis is a proven strategy for killing bacteria with antibiotics. The assembly of PG requires disaccharide-pentapeptide building blocks attached to a polyisoprene lipid carrier called lipid II. Although the stages of lipid II synthesis are known, the identity of the essential flippase that translocates it across the cytoplasmic membrane for PG polymerization is unclear. We developed an assay for lipid II flippase activity and used a chemical genetic strategy to rapidly and specifically block flippase function. We combined these approaches to demonstrate that MurJ is the lipid II flippase in Escherichia coli.

Copyright © 2014, American Association for the Advancement of Science.

PMID:
25013077
[PubMed - indexed for MEDLINE]
PMCID:
PMC4163187
Free PMC Article
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