Role of the purine repressor in the regulation of pyrimidine gene expression in Escherichia coli K-12.

Academic Article


  • The pyrC and pyrD genes of Escherichia coli K-12 encode the pyrimidine biosynthetic enzymes dihydroorotase and dihydroorotate dehydrogenase, respectively. A highly conserved sequence in the promoter regions of these two genes is similar to the pur operator, which is the binding site for the purine repressor (PurR). In this study, we examined the role of PurR in the regulation of pyrC and pyrD expression. Our results show that pyrC and pyrD expression was repressed approximately twofold in cells grown in the presence of adenine [corrected] through a mechanism requiring PurR. A mutation, designated pyrCp926, which alters a 6-base-pair region within the conserved sequence in the pyrC promoter eliminated PurR-mediated repression of pyrC expression. This result indicates that PurR binds to the pyrC (and presumably to the pyrD) conserved sequence and inhibits transcriptional initiation. We also demonstrated that the pyrCp926 mutation had no effect on pyrimidine-mediated regulation of pyrC expression, indicating that pyrimidine and purine effectors act through independent mechanisms to control the expression of the pyrC and pyrD genes.
  • Published In


  • Amidohydrolases, Base Sequence, Dihydroorotase, Dihydroorotate Oxidase, Escherichia coli, Gene Expression Regulation, Enzymologic, Molecular Sequence Data, Mutation, Oxidoreductases, Purines, Pyrimidine Nucleotides, Pyrimidines, Repressor Proteins, Transcription Factors
  • Digital Object Identifier (doi)

    Author List

  • Wilson HR; Turnbough CL
  • Start Page

  • 3208
  • End Page

  • 3213
  • Volume

  • 172
  • Issue

  • 6