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Gene Review

rpoB  -  DNA-directed RNA polymerase subunit beta

Escherichia coli UTI89

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Disease relevance of rpoB


High impact information on rpoB


Biological context of rpoB

  • Five recombinant plasmids, pBK2646, pBK611, pRC3, pRC4 and pRC5, carrying rpoB rifampicin-resistant RNA-polymerase genes were obtained [9].
  • Their mutagenic potentials were assayed using the chromosomal rpoB gene as a mutagenesis target [10].

Other interactions of rpoB

  • Most of the mutations that occurred in H. pylori mutY mutants, as examined by rpoB sequence changes that confer rifampicin resistance, are GC to TA transversions [11].

Analytical, diagnostic and therapeutic context of rpoB

  • Here, we used site-directed mutagenesis followed by selection on Rif to search for RifR mutations in the evolutionarily conserved segment of rpoB around codon 146 [12].
  • The sequence analysis of these plasmids revealed certain structural changes in the rpoB gene which specify corresponding alterations in the beta-subunit of RNA polymerase [9].
  • The locations of four of the eleven rpoB amber mutations that are strongly polar on expression of the downstream rpoC gene have been determined through a combination of MaeI mapping, PCR amplification and DNA sequencing [13].


  1. Archaebacterial DNA-dependent RNA polymerases testify to the evolution of the eukaryotic nuclear genome. Pühler, G., Leffers, H., Gropp, F., Palm, P., Klenk, H.P., Lottspeich, F., Garrett, R.A., Zillig, W. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  2. Emergence of rifampin-resistant Rhodococcus equi with several types of mutations in the rpoB gene among AIDS patients in northern Thailand. Asoh, N., Watanabe, H., Fines-Guyon, M., Watanabe, K., Oishi, K., Kositsakulchai, W., Sanchai, T., Kunsuikmengrai, K., Kahintapong, S., Khantawa, B., Tharavichitkul, P., Sirisanthana, T., Nagatake, T. J. Clin. Microbiol. (2003) [Pubmed]
  3. Nucleotide sequence of the Staphylococcus aureus RNA polymerase rpoB gene and comparison of its predicted amino acid sequence with those of other bacteria. Aboshkiwa, M., Rowland, G., Coleman, G. Biochim. Biophys. Acta (1995) [Pubmed]
  4. Transcription coupled nucleotide excision repair by isolated Escherichia coli membrane-associated nucleoids. ClGL, n.u.l.l., Kovalsky, O., Grossman, L. Nucleic Acids Res. (1998) [Pubmed]
  5. RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit to the beta subunit of Escherichia coli RNA polymerase. Falkenburg, D., Dworniczak, B., Faust, D.M., Bautz, E.K. J. Mol. Biol. (1987) [Pubmed]
  6. Insertional mutagenesis of a plasmid-borne Escherichia coli rpoB gene reveals alterations that inhibit beta-subunit assembly into RNA polymerase. Landick, R., Colwell, A., Stewart, J. J. Bacteriol. (1990) [Pubmed]
  7. Direct evidence for autogenous regulation of the Escherichia coli genes rpoBC in vivo. Meek, D.W., Hayward, R.S. Mol. Gen. Genet. (1986) [Pubmed]
  8. Sequence analysis of an aphid endosymbiont DNA fragment containing rpoB (beta-subunit of RNA polymerase) and portions of rplL and rpoC. Clark, M.A., Baumann, L., Baumann, P. Curr. Microbiol. (1992) [Pubmed]
  9. RNA polymerase rifampicin resistance mutations in Escherichia coli: sequence changes and dominance. Ovchinnikov, Y.A., Monastyrskaya, G.S., Guriev, S.O., Kalinina, N.F., Sverdlov, E.D., Gragerov, A.I., Bass, I.A., Kiver, I.F., Moiseyeva, E.P., Igumnov, V.N., Mindlin, S.Z., Nikiforov, V.G., Khesin, R.B. Mol. Gen. Genet. (1983) [Pubmed]
  10. In vivo mutagenicities of damaged nucleotides produced by nitric oxide and ionizing radiation. Hori, M., Ishiguro, C., Harashima, H., Kamiya, H. Biol. Pharm. Bull. (2005) [Pubmed]
  11. Role of a MutY DNA glycosylase in combating oxidative DNA damage in Helicobacter pylori. Eutsey, R., Wang, G., Maier, R.J. DNA Repair (Amst.) (2007) [Pubmed]
  12. RifR mutations in the beginning of the Escherichia coli rpoB gene. Severinov, K., Soushko, M., Goldfarb, A., Nikiforov, V. Mol. Gen. Genet. (1994) [Pubmed]
  13. Physical mapping of a collection of Mael-generating amber mutations in the beta gene of Escherichia coli RNA polymerase and the functional effect of internal deletions constructed through their manipulation. Buyukuslu, N., Trigwell, S.M., Lim, P.P., Fujita, N., Ishihama, A., Ralphs, N.T., Glass, R.E. Genes Funct. (1997) [Pubmed]
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