Heat shock response in Escherichia coli promotes assembly of plasmid encoded RNA polymerase beta-subunit into RNA polymerase

Mol Gen Genet. 1989 Apr;216(2-3):469-74. doi: 10.1007/BF00334392.


Escherichia coli cells, carrying a rifampicin sensitive RNA polymerase beta-subunit gene in the chromosome and a rifampicin resistant beta-subunit gene placed under the control of a strong promoter in a multicopy plasmid, are unable to grow in the presence of rifampicin, despite the accumulation of large quantities of the resistant subunit. A major portion of the overproduced subunit is found in an insoluble form. Conditions known to induce the heat shock proteins (hsps), e.g. elevated temperature or the presence of ethanol in the growth medium, increase the amount of the plasmid-borne beta-subunit which apparently assembles into active RNA polymerase and makes the plasmid bearing cells rifampicin resistant. Alternatively, plasmid-borne subunits assemble into RNA polymerase with low efficiency in rpoH mutant cells known to have reduced level of hsps. We suggest that the plasmid-borne subunit is poorly assembled into RNA polymerase and that hsps promote the assembly by interfering with beta-subunit aggregation.

MeSH terms

  • DNA-Directed RNA Polymerases / biosynthesis*
  • DNA-Directed RNA Polymerases / genetics
  • Drug Resistance, Microbial / genetics
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Genes, Bacterial
  • Heat-Shock Proteins / biosynthesis*
  • Heat-Shock Proteins / genetics
  • Hot Temperature
  • Mutation
  • Plasmids
  • Protein Conformation
  • Rifampin / pharmacology


  • Heat-Shock Proteins
  • DNA-Directed RNA Polymerases
  • Rifampin