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

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 lipi...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2014-07, Vol.345 (6193), p.220-222
Main Authors: Sham, Lok-To, Butler, Emily K, Lebar, Matthew D, Kahne, Daniel, Bernhardt, Thomas G, Ruiz, Natividad
Format: Article
Language:English
Subjects:
Cell Wall - metabolism
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - antagonists & inhibitors
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - physiology
Mesylates - pharmacology
Models, Molecular
Peptidoglycan - biosynthesis
Peptidoglycan - chemistry
Phospholipid Transfer Proteins - antagonists & inhibitors
Phospholipid Transfer Proteins - chemistry
Phospholipid Transfer Proteins - physiology
Protein Conformation
Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives
Uridine Diphosphate N-Acetylmuramic Acid - metabolism
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Summary: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.
ISSN:1095-9203
DOI:10.1126/science.1254522