Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1991 Jul;173(14):4417–4423. doi: 10.1128/jb.173.14.4417-4423.1991

Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12.

V Stewart 1, J T Lin 1, B L Berg 1
PMCID: PMC208104  PMID: 1648557

Abstract

Enterobacteria synthesize two formate dehydrogenases, formate dehydrogenase-N (encoded by fdnGHI) and formate dehydrogenase H (encoded by fdhF). Previous work has identified two rha-linked Salmonella typhimurium genes, fdnB and fdnC, which are required primarily for formate dehydrogenase-N activity. Analogous mutants, termed fdhD and fdhE, have been isolated in Escherichia coli. We used gene fusions between fdnG, the structural gene for the large subunit of formate dehydrogenase-N, and lacZ, the structural gene for beta-galactosidase, to examine E. coli fdnGHI operon expression in fdhD and fdhE insertion mutants. Expression of the phi (fdnG-lacZ) gene fusions was little affected by these insertions, suggesting that fdhD and fdhE do not control transcription or UGA decoding of the formate dehydrogenase-N structural genes. Our complementation tests, with cloned E. coli fdhD and fdhE genes, indicate that the S. typhimurium fdnC and fdnB genes are functionally homologous to the E. coli fdhD and fdhE genes, respectively.

Full text

PDF
4421

Selected References

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

  1. Arps P. J., Winkler M. E. Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette. J Bacteriol. 1987 Mar;169(3):1061–1070. doi: 10.1128/jb.169.3.1061-1070.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barrett E. L., Jackson C. E., Fukumoto H. T., Chang G. W. Formate dehydrogenase mutants of Salmonella typhimurium: a new medium for their isolation and new mutant classes. Mol Gen Genet. 1979;177(1):95–101. doi: 10.1007/BF00267258. [DOI] [PubMed] [Google Scholar]
  3. Barrett E. L., Riggs D. L. Salmonella typhimurium mutants defective in the formate dehydrogenase linked to nitrate reductase. J Bacteriol. 1982 Feb;149(2):554–560. doi: 10.1128/jb.149.2.554-560.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Berg B. L., Stewart V. Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics. 1990 Aug;125(4):691–702. doi: 10.1093/genetics/125.4.691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brewer J. H., Allgeier D. L. Safe Self-contained Carbon Dioxide-Hydrogen Anaerobic System. Appl Microbiol. 1966 Nov;14(6):985–988. doi: 10.1128/am.14.6.985-988.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bullas L. R., Ryu J. I. Salmonella typhimurium LT2 strains which are r- m+ for all three chromosomally located systems of DNA restriction and modification. J Bacteriol. 1983 Oct;156(1):471–474. doi: 10.1128/jb.156.1.471-474.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Böhm R., Sauter M., Böck A. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol Microbiol. 1990 Feb;4(2):231–243. doi: 10.1111/j.1365-2958.1990.tb00590.x. [DOI] [PubMed] [Google Scholar]
  8. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  9. Chang A. C., Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol. 1978 Jun;134(3):1141–1156. doi: 10.1128/jb.134.3.1141-1156.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Forchhammer K., Leinfelder W., Böck A. Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature. 1989 Nov 23;342(6248):453–456. doi: 10.1038/342453a0. [DOI] [PubMed] [Google Scholar]
  11. Groisman E. A., Casadaban M. J. Mini-mu bacteriophage with plasmid replicons for in vivo cloning and lac gene fusing. J Bacteriol. 1986 Oct;168(1):357–364. doi: 10.1128/jb.168.1.357-364.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hughes K. T., Roth J. R. Transitory cis complementation: a method for providing transposition functions to defective transposons. Genetics. 1988 May;119(1):9–12. doi: 10.1093/genetics/119.1.9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Iuchi S., Lin E. C. The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3901–3905. doi: 10.1073/pnas.84.11.3901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kohara Y., Akiyama K., Isono K. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell. 1987 Jul 31;50(3):495–508. doi: 10.1016/0092-8674(87)90503-4. [DOI] [PubMed] [Google Scholar]
  15. Leinfelder W., Forchhammer K., Veprek B., Zehelein E., Böck A. In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product. Proc Natl Acad Sci U S A. 1990 Jan;87(2):543–547. doi: 10.1073/pnas.87.2.543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Leinfelder W., Forchhammer K., Zinoni F., Sawers G., Mandrand-Berthelot M. A., Böck A. Escherichia coli genes whose products are involved in selenium metabolism. J Bacteriol. 1988 Feb;170(2):540–546. doi: 10.1128/jb.170.2.540-546.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Leinfelder W., Zehelein E., Mandrand-Berthelot M. A., Böck A. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature. 1988 Feb 25;331(6158):723–725. doi: 10.1038/331723a0. [DOI] [PubMed] [Google Scholar]
  18. Mandrand-Berthelot M. A., Couchoux-Luthaud G., Santini C. L., Giordano G. Mutants of Escherichia coli specifically deficient in respiratory formate dehydrogenase activity. J Gen Microbiol. 1988 Dec;134(12):3129–3139. doi: 10.1099/00221287-134-12-3129. [DOI] [PubMed] [Google Scholar]
  19. Paveglio M. T., Tang J. S., Unger R. E., Barrett E. L. Formate-nitrate respiration in Salmonella typhimurium: studies of two rha-linked fdn genes. J Bacteriol. 1988 Jan;170(1):213–217. doi: 10.1128/jb.170.1.213-217.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pecher A., Zinoni F., Böck A. The seleno-polypeptide of formic dehydrogenase (formate hydrogen-lyase linked) from Escherichia coli: genetic analysis. Arch Microbiol. 1985 May;141(4):359–363. doi: 10.1007/BF00428850. [DOI] [PubMed] [Google Scholar]
  21. Schlindwein C., Giordano G., Santini C. L., Mandrand M. A. Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase. J Bacteriol. 1990 Oct;172(10):6112–6121. doi: 10.1128/jb.172.10.6112-6121.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Simons R. W., Houman F., Kleckner N. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene. 1987;53(1):85–96. doi: 10.1016/0378-1119(87)90095-3. [DOI] [PubMed] [Google Scholar]
  23. Spiro S., Guest J. R. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol Rev. 1990 Aug;6(4):399–428. doi: 10.1111/j.1574-6968.1990.tb04109.x. [DOI] [PubMed] [Google Scholar]
  24. Stewart G. S., Lubinsky-Mink S., Jackson C. G., Cassel A., Kuhn J. pHG165: a pBR322 copy number derivative of pUC8 for cloning and expression. Plasmid. 1986 May;15(3):172–181. doi: 10.1016/0147-619x(86)90035-1. [DOI] [PubMed] [Google Scholar]
  25. Stewart V., Berg B. L. Influence of nar (nitrate reductase) genes on nitrate inhibition of formate-hydrogen lyase and fumarate reductase gene expression in Escherichia coli K-12. J Bacteriol. 1988 Oct;170(10):4437–4444. doi: 10.1128/jb.170.10.4437-4444.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Stewart V., MacGregor C. H. Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci. J Bacteriol. 1982 Aug;151(2):788–799. doi: 10.1128/jb.151.2.788-799.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Stewart V. Nitrate respiration in relation to facultative metabolism in enterobacteria. Microbiol Rev. 1988 Jun;52(2):190–232. doi: 10.1128/mr.52.2.190-232.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Stewart V., Parales J., Jr Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol. 1988 Apr;170(4):1589–1597. doi: 10.1128/jb.170.4.1589-1597.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Stewart V. Requirement of Fnr and NarL functions for nitrate reductase expression in Escherichia coli K-12. J Bacteriol. 1982 Sep;151(3):1320–1325. doi: 10.1128/jb.151.3.1320-1325.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Way J. C., Davis M. A., Morisato D., Roberts D. E., Kleckner N. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene. 1984 Dec;32(3):369–379. doi: 10.1016/0378-1119(84)90012-x. [DOI] [PubMed] [Google Scholar]
  31. Winans S. C., Elledge S. J., Krueger J. H., Walker G. C. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J Bacteriol. 1985 Mar;161(3):1219–1221. doi: 10.1128/jb.161.3.1219-1221.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wu L. F., Mandrand-Berthelot M. A., Waugh R., Edmonds C. J., Holt S. E., Boxer D. H. Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli. Mol Microbiol. 1989 Dec;3(12):1709–1718. doi: 10.1111/j.1365-2958.1989.tb00156.x. [DOI] [PubMed] [Google Scholar]
  33. Zinoni F., Birkmann A., Leinfelder W., Böck A. Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci U S A. 1987 May;84(10):3156–3160. doi: 10.1073/pnas.84.10.3156. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES