Control of the LexA regulon by pH: evidence for a reversible inactivation of the LexA repressor during the growth cycle of Escherichia coli

Mol Microbiol. 1994 May;12(4):621-9. doi: 10.1111/j.1365-2958.1994.tb01049.x.


The LexA repressor controls the expression of several genes, including lexA, recA, and sfiA, which are induced when exponentially growing bacteria are exposed to DNA-damaging agents. Induction of this so-called SOS response takes place while LexA is cleaved in a reaction that requires the RecA protein and damaged DNA. We have shown that large fluctuations in the cellular concentration of the LexA repressor and in the rate of transcription of the sfiA gene also occur spontaneously during bacterial growth in complex medium such as LB. The possibility that changes in external or internal pH may explain these fluctuations has been explored. A consistent pattern was established whereby conditions leading to either increased or decreased pH were associated with altered expression of the lexA and sfiA genes. These data can be explained by a model in which the LexA repressor exists in either of two forms in equilibrium: a form favoured at homeostatic internal pH, which has a low affinity for the operators of LexA-controlled genes; and a form accumulated in response to a transient decrease in internal pH, which has a high affinity for operators.

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • DNA, Bacterial / drug effects
  • DNA, Bacterial / metabolism
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism
  • Gene Expression Regulation, Bacterial / drug effects
  • Hydrogen-Ion Concentration
  • Kinetics
  • Propionates / pharmacology
  • Regulon*
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism
  • SOS Response, Genetics / genetics
  • SOS Response, Genetics / physiology
  • Serine Endopeptidases*


  • Bacterial Proteins
  • DNA, Bacterial
  • LexA protein, Bacteria
  • Propionates
  • Repressor Proteins
  • Serine Endopeptidases
  • propionic acid