HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

Role of precursor translocation in coordination of murein and phospholipid synthesis in Escherichia coli.

Abstract
Inhibition of phospholipid synthesis in Escherichia coli by either cerulenin treatment or glycerol starvation of a glycerol-auxotrophic mutant resulted in a concomitant block of murein synthesis. The intracellular pool of cytoplasmic and lipid-linked murein precursors was not affected by an inhibition of phospholipid synthesis, nor was the activity of the penicillin-binding proteins. In addition, a decrease in the activity of the two lipoprotein murein hydrolases, the lytic transglycosylases A and B, could not be demonstrated. The indirect inhibition of murein synthesis by cerulenin resulted in a 68% decrease of trimeric muropeptide structures, proposed to represent the attachment points of newly added murein. Importantly, inhibition of phospholipid synthesis also inhibited O-antigen synthesis with a sensitivity and kinetics similar to those of murein synthesis. It is concluded that the step common for murein and O-antigen synthesis, the translocation of the respective bactoprenolphosphate-linked precursor molecules, is affected by an inhibition of phospholipid synthesis. Consistent with this assumption, it was shown that murein synthesis no longer depends on ongoing phospholipid synthesis in ether-permeabilized cells. We propose that the assembly of a murein-synthesizing machinery, a multienzyme complex consisting of murein hydrolases and synthases, at specific sites of the membrane, where integral membrane proteins such as RodA and FtsW facilitate the translocation of the lipid-linked murein precursors to the periplasm, depends on ongoing phospholipid synthesis. This would explain the well-known phenomenon that both murein synthesis and antibiotic-induced autolysis depend on phospholipid synthesis and thereby indirectly on the stringent control.
AuthorsK Ehlert, J V Höltje
JournalJournal of bacteriology (J Bacteriol) Vol. 178 Issue 23 Pg. 6766-71 (Dec 1996) ISSN: 0021-9193 [Print] United States
PMID8955294 (Publication Type: Journal Article)
Chemical References
  • Bacterial Proteins
  • Carrier Proteins
  • O Antigens
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • Phospholipids
  • Protein Precursors
  • Cerulenin
  • Ampicillin
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • N-Acetylmuramoyl-L-alanine Amidase
Topics
  • Ampicillin (metabolism)
  • Bacterial Proteins
  • Biological Transport
  • Carrier Proteins (metabolism)
  • Cell Membrane Permeability
  • Cerulenin (pharmacology)
  • Escherichia coli (metabolism)
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase (metabolism)
  • N-Acetylmuramoyl-L-alanine Amidase (metabolism)
  • O Antigens (biosynthesis)
  • Penicillin-Binding Proteins
  • Peptidoglycan (biosynthesis, chemistry)
  • Peptidyl Transferases
  • Phospholipids (biosynthesis)
  • Protein Precursors (metabolism)

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: