Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1989 Dec 11;17(23):9979–9991. doi: 10.1093/nar/17.23.9979

Nucleotide sequence of katF of Escherichia coli suggests KatF protein is a novel sigma transcription factor.

M R Mulvey 1, P C Loewen 1
PMCID: PMC335226  PMID: 2690013

Abstract

The katF gene of Escherichia coli has been sequenced revealing a 1086 base pair open reading frame from which the sequence of a 362 amino acid protein has been deduced. The direction of transcription of katF was confirmed by expression of the gene cloned in both directions behind a T7 promoter. The KatF protein expressed in vitro migrates with an apparent size of 42 kDa. Comparison of the katF sequence to the sequence of rpoD, which encodes the sigma subunit of RNA polymerase, revealed a 181 bp region with 65% homology and a 38 bp segment that was 87% homologous. A 62 amino acid region of the predicted KatF protein sequence was found to be 85% homologous to the corresponding sequence of sigma 70, including a segment implicated in core polymerase binding. Homology was also observed with the heat shock regulatory protein encoded by htpR.

Full text

PDF
9979

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boyer H. W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. doi: 10.1016/0022-2836(69)90288-5. [DOI] [PubMed] [Google Scholar]
  3. Burton Z., Burgess R. R., Lin J., Moore D., Holder S., Gross C. A. The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12. Nucleic Acids Res. 1981 Jun 25;9(12):2889–2903. doi: 10.1093/nar/9.12.2889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Christman M. F., Morgan R. W., Jacobson F. S., Ames B. N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 1985 Jul;41(3):753–762. doi: 10.1016/s0092-8674(85)80056-8. [DOI] [PubMed] [Google Scholar]
  5. Claiborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J Biol Chem. 1979 May 25;254(10):4245–4252. [PubMed] [Google Scholar]
  6. Claiborne A., Malinowski D. P., Fridovich I. Purification and characterization of hydroperoxidase II of Escherichia coli B. J Biol Chem. 1979 Nov 25;254(22):11664–11668. [PubMed] [Google Scholar]
  7. Eisenstark A., Perrot G. Catalase has only a minor role in protection against near-ultraviolet radiation damage in bacteria. Mol Gen Genet. 1987 Apr;207(1):68–72. doi: 10.1007/BF00331492. [DOI] [PubMed] [Google Scholar]
  8. Finn G. J., Condon S. Regulation of catalase synthesis in Salmonella typhimurium. J Bacteriol. 1975 Aug;123(2):570–579. doi: 10.1128/jb.123.2.570-579.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Grosjean H., Fiers W. Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene. 1982 Jun;18(3):199–209. doi: 10.1016/0378-1119(82)90157-3. [DOI] [PubMed] [Google Scholar]
  10. Helmann J. D., Chamberlin M. J. Structure and function of bacterial sigma factors. Annu Rev Biochem. 1988;57:839–872. doi: 10.1146/annurev.bi.57.070188.004203. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Landick R., Vaughn V., Lau E. T., VanBogelen R. A., Erickson J. W., Neidhardt F. C. Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor. Cell. 1984 Aug;38(1):175–182. doi: 10.1016/0092-8674(84)90538-5. [DOI] [PubMed] [Google Scholar]
  13. Lee Y. M., Lee S. C. A DNA sequencing strategy. Anal Biochem. 1988 Dec;175(2):521–524. doi: 10.1016/0003-2697(88)90577-5. [DOI] [PubMed] [Google Scholar]
  14. Lesley S. A., Burgess R. R. Characterization of the Escherichia coli transcription factor sigma 70: localization of a region involved in the interaction with core RNA polymerase. Biochemistry. 1989 Sep 19;28(19):7728–7734. doi: 10.1021/bi00445a031. [DOI] [PubMed] [Google Scholar]
  15. Loewen P. C. Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity. J Bacteriol. 1984 Feb;157(2):622–626. doi: 10.1128/jb.157.2.622-626.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Loewen P. C., Switala J., Triggs-Raine B. L. Catalases HPI and HPII in Escherichia coli are induced independently. Arch Biochem Biophys. 1985 Nov 15;243(1):144–149. doi: 10.1016/0003-9861(85)90782-9. [DOI] [PubMed] [Google Scholar]
  17. Loewen P. C., Switala J., Triggs-Raine B. L. Catalases HPI and HPII in Escherichia coli are induced independently. Arch Biochem Biophys. 1985 Nov 15;243(1):144–149. doi: 10.1016/0003-9861(85)90782-9. [DOI] [PubMed] [Google Scholar]
  18. Loewen P. C., Triggs B. L. Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. J Bacteriol. 1984 Nov;160(2):668–675. doi: 10.1128/jb.160.2.668-675.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Loewen P. C., Triggs B. L., George C. S., Hrabarchuk B. E. Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli. J Bacteriol. 1985 May;162(2):661–667. doi: 10.1128/jb.162.2.661-667.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mulvey M. R., Sorby P. A., Triggs-Raine B. L., Loewen P. C. Cloning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli. Gene. 1988 Dec 20;73(2):337–345. doi: 10.1016/0378-1119(88)90498-2. [DOI] [PubMed] [Google Scholar]
  21. Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
  22. Sak B. D., Eisenstark A., Touati D. Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product. Proc Natl Acad Sci U S A. 1989 May;86(9):3271–3275. doi: 10.1073/pnas.86.9.3271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sammartano L. J., Tuveson R. W., Davenport R. Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus. J Bacteriol. 1986 Oct;168(1):13–21. doi: 10.1128/jb.168.1.13-21.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sammartano L. J., Tuveson R. W. Escherichia coli xthA mutants are sensitive to inactivation by broad-spectrum near-UV (300- to 400-nm) radiation. J Bacteriol. 1983 Nov;156(2):904–906. doi: 10.1128/jb.156.2.904-906.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Saporito S. M., Smith-White B. J., Cunningham R. P. Nucleotide sequence of the xth gene of Escherichia coli K-12. J Bacteriol. 1988 Oct;170(10):4542–4547. doi: 10.1128/jb.170.10.4542-4547.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Schreier P. H., Cortese R. A fast and simple method for sequencing DNA cloned in the single-stranded bacteriophage M13. J Mol Biol. 1979 Mar 25;129(1):169–172. doi: 10.1016/0022-2836(79)90068-8. [DOI] [PubMed] [Google Scholar]
  28. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Stragier P., Parsot C., Bouvier J. Two functional domains conserved in major and alternate bacterial sigma factors. FEBS Lett. 1985 Jul 22;187(1):11–15. doi: 10.1016/0014-5793(85)81203-5. [DOI] [PubMed] [Google Scholar]
  30. Tabor S., Richardson C. C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci U S A. 1985 Feb;82(4):1074–1078. doi: 10.1073/pnas.82.4.1074. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Weber K., Pringle J. R., Osborn M. Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 1972;26:3–27. doi: 10.1016/s0076-6879(72)26003-7. [DOI] [PubMed] [Google Scholar]
  32. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES