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. 1995 Aug;177(15):4528–4531. doi: 10.1128/jb.177.15.4528-4531.1995

Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat.

V Bianchi 1, E Haggård-Ljungquist 1, E Pontis 1, P Reichard 1
PMCID: PMC177208  PMID: 7635836

Abstract

Ferredoxin (flavodoxin) NADP+ oxidoreductase participates in methionine biosynthesis and in the function of two anaerobic enzymes, pyruvate formate-lyase and ribonucleotide reductase. We prepared insertion mutants of Escherichia coli lacking a functional enzyme. They do not require methionine and they grow well anaerobically, but they show increased sensitivity to paraquat.

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Selected References

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  1. Andrews S. C., Shipley D., Keen J. N., Findlay J. B., Harrison P. M., Guest J. R. The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases. FEBS Lett. 1992 May 18;302(3):247–252. doi: 10.1016/0014-5793(92)80452-m. [DOI] [PubMed] [Google Scholar]
  2. Bianchi V., Eliasson R., Fontecave M., Mulliez E., Hoover D. M., Matthews R. G., Reichard P. Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase. Biochem Biophys Res Commun. 1993 Dec 15;197(2):792–797. doi: 10.1006/bbrc.1993.2548. [DOI] [PubMed] [Google Scholar]
  3. Bianchi V., Reichard P., Eliasson R., Pontis E., Krook M., Jörnvall H., Haggård-Ljungquist E. Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein. J Bacteriol. 1993 Mar;175(6):1590–1595. doi: 10.1128/jb.175.6.1590-1595.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blaschkowski H. P., Neuer G., Ludwig-Festl M., Knappe J. Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase. Eur J Biochem. 1982 Apr;123(3):563–569. [PubMed] [Google Scholar]
  5. Calero S., Fernandez de Henestrosa A. R., Barbé J. Molecular cloning, sequence and regulation of expression of the recA gene of the phototrophic bacterium Rhodobacter sphaeroides. Mol Gen Genet. 1994 Jan;242(1):116–120. doi: 10.1007/BF00277356. [DOI] [PubMed] [Google Scholar]
  6. Demple B., Amábile-Cuevas C. F. Redox redux: the control of oxidative stress responses. Cell. 1991 Nov 29;67(5):837–839. doi: 10.1016/0092-8674(91)90355-3. [DOI] [PubMed] [Google Scholar]
  7. Eliasson R., Pontis E., Fontecave M., Gerez C., Harder J., Jörnvall H., Krook M., Reichard P. Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli. J Biol Chem. 1992 Dec 15;267(35):25541–25547. [PubMed] [Google Scholar]
  8. Fujii K., Huennekens F. M. Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system. J Biol Chem. 1974 Nov 10;249(21):6745–6753. [PubMed] [Google Scholar]
  9. Gaudu P., Fontecave M. The NADPH: sulfite reductase of Escherichia coli is a paraquat reductase. Eur J Biochem. 1994 Dec 1;226(2):459–463. doi: 10.1111/j.1432-1033.1994.tb20070.x. [DOI] [PubMed] [Google Scholar]
  10. Herrero M., de Lorenzo V., Timmis K. N. Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria. J Bacteriol. 1990 Nov;172(11):6557–6567. doi: 10.1128/jb.172.11.6557-6567.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Karplus P. A., Daniels M. J., Herriott J. R. Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science. 1991 Jan 4;251(4989):60–66. [PubMed] [Google Scholar]
  12. Liochev S. I., Hausladen A., Beyer W. F., Jr, Fridovich I. NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1328–1331. doi: 10.1073/pnas.91.4.1328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Morimyo M. Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12. J Bacteriol. 1988 May;170(5):2136–2142. doi: 10.1128/jb.170.5.2136-2142.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Oka A., Sugisaki H., Takanami M. Nucleotide sequence of the kanamycin resistance transposon Tn903. J Mol Biol. 1981 Apr 5;147(2):217–226. doi: 10.1016/0022-2836(81)90438-1. [DOI] [PubMed] [Google Scholar]
  15. Sasaki I., Bertani G. Growth abnormalities in Hfr derivatives of Escherichia coli strain C. J Gen Microbiol. 1965 Sep;40(3):365–376. doi: 10.1099/00221287-40-3-365. [DOI] [PubMed] [Google Scholar]
  16. Sun X., Eliasson R., Pontis E., Andersson J., Buist G., Sjöberg B. M., Reichard P. Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme. J Biol Chem. 1995 Feb 10;270(6):2443–2446. doi: 10.1074/jbc.270.6.2443. [DOI] [PubMed] [Google Scholar]
  17. Truniger V., Boos W., Sweet G. Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri. J Bacteriol. 1992 Nov;174(21):6981–6991. doi: 10.1128/jb.174.21.6981-6991.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. de Lorenzo V., Herrero M., Jakubzik U., Timmis K. N. Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria. J Bacteriol. 1990 Nov;172(11):6568–6572. doi: 10.1128/jb.172.11.6568-6572.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]

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