Novel regulator PgrR for switch control of peptidoglycan recycling in Escherichia coli

Genes Cells. 2013 Feb;18(2):123-34. doi: 10.1111/gtc.12026. Epub 2013 Jan 10.


Peptidoglycan (PG), also designated as murein, forms a skeletal mesh within the periplasm of bacterial membrane. PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill-defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties are either recycled or used as self-generated nutrients for cell growth. At present, the control of PG degradation remains uncharacterized. Using the Genomic SELEX screening system, we identified an uncharacterized transcription factor YcjZ is a repressor of the expression of the initial step enzymes for PG peptide degradation. Under nutrient starvation, the genes encoding the enzymes for PG peptide degradation are derepressed so as to generate amino acids but are tightly repressed at high osmotic conditions so as to maintain the rigid membrane for withstanding the turgor. Taken together, we propose to rename YcjZ as PgrR (regulator of peptide glycan recycling).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial
  • Genes, Reporter
  • Nucleotide Motifs
  • Operator Regions, Genetic
  • Peptidoglycan / metabolism*
  • Protein Binding
  • Proteolysis
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transcription, Genetic


  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Peptidoglycan
  • PgrR protein, E coli
  • Transcription Factors