Journal of Microbiology

The Microbiological Society of Korea (한국미생물학회)
권호 표지

Regulation of the sufABCDSE Operon by Fur

  • Lee, Joon-Hee (Laboratory of Molecular Microbiology, School of Biological Sciences) ;
  • Yeo, Won-Sik (Laboratory of Molecular Microbiology, School of Biological Sciences) ;
  • Roe, Jung-Hye (Institute of Microbiology, Seoul National University)
  • Published : 2003.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

A promoter that is inducible by paraquat and menadione, the superoxide generators, independently of soxRS has been found in front of the sufABCDSE operon in Escherichia coli. Based on the observation that SufA is a holomog of IscA that functions in the assembly of iron sulfur cluster and the sufA promoter (sufAp) contains a putative Fur-binding consensus, we investigated whether this gene is regulated by Fur, a ferric uptake regulator, When examined in several sufAp-lacZ chromosomal fusion strains, sufAp was induced by EDTA, an iron chelator and a well-known Fur-inducer, The basal level of sufA expression increased dramatically in fur mutant, suggesting repression of sufAp by Fur. The derepression in fur mutant and EDTA-induction of sufA expression required nucleotides up to -61, where a putative Fur box is located. Purified Fur protein bound to the DNA fragment containing the putative Fur box between -35 and -10 promoter elements. The regulation by Fur and menadione induction of sufAp acted independently. The rpoS mutation increased sufA induction by menadione, suggesting that the stationary sigma factor RpoS acts negatively on sufA induction.

Keywords

References

  1. Biochemistry v.38 The ferric uptake regulation (Fur) repressor is a zinc metalloprotein Althaus,E.W.;C.E.Outten;K.E.Olson;H.Cao;T.V.O'Halloran https://doi.org/10.1021/bi982788s
  2. J. Biol. Chem. v.271 Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxyacid dehydratase Flint,D.H.
  3. Biochemistry v.39 Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase Fujii,T.;M.Maeda;H.Mihara;T.Kurihara;N.Esaki;Y.Hata https://doi.org/10.1021/bi991732a
  4. J. Bacteriol. v.171 A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by superoxide stress Greenberg,J.T.;B.Demple
  5. Proc. Natl. Acad. Sci. USA. v.87 Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli Greenberg,J.T.;P.Monach;J.H.Chou;P.D.Josephy;B.Demple https://doi.org/10.1073/pnas.87.16.6181
  6. J. Bacteriol. v.173 Activation of oxidative stress genes by mutations at the soxQ/cfxB/marA locus of Escherichia coli Greenberg,J.T.;J.H.Chou;P.Monachch;B.Demple
  7. Mol. Cell. Biol. v.20 Roles of Sacharomyces cerevisiase ISA1 and ISA2 in iron homeostatsis Jensen,L.T.;V.C.Culotta https://doi.org/10.1128/MCB.20.11.3918-3927.2000
  8. J. Biol. Chem. v.275 Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function Kaut,A.;H.lange;K.Diekert;G.Kispal;R.Lill https://doi.org/10.1074/jbc.M909502199
  9. J. Microbiol. v.35 Isolation and characterization of paraquat-inducible promoters from Escherichia coli Lee,J.H.;J.H.Roe
  10. Free Radic. Biol. Med. v.24 Mechanism of regulation of 8-hydroxyguanine endonuclease by oxidative stress: roles of FNR, ArcA, and Fur Lee,H.S.;Y.S.Lee;H.S.Kim;J.Y.Choi;H.M.Hassan;M.H.Chung https://doi.org/10.1016/S0891-5849(97)00427-9
  11. J. Bacteriol. v.179 Paraquat regulation of hmp (Flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S Membrillo-Hern$\ `{a}$ndez,J.;S.O.Kim;G.M.Cook;R.K.Poole
  12. J. Biol. Chem. v.272 Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme Mihara,H.;T.Kurihara;T.Yoshimura;K.Soda;N.Esaki https://doi.org/10.1074/jbc.272.36.22417
  13. A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria Miller,J.H.
  14. Mol. Microbiol. v.39 SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase Nachin,L.;M.El Hassouni;L.Loiseau;D.Expert;F.Barras https://doi.org/10.1046/j.1365-2958.2001.02288.x
  15. EMBO J. v.22 SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress Nachin,L.;L.Loiseau;D.Expert;F.Barras https://doi.org/10.1093/emboj/cdg061
  16. J. Biol. Chem. v.278 SufA from Erwinia chrysanthemi: Characterization of a scaffold protein required for ironsulfur cluster assembly Ollagnier-De Choudens,S.;L.nachin;Y.Sanakis;L.Loiseau;F.Barras;M.Fontecave https://doi.org/10.1074/jbc.M300285200
  17. J. Bacteriol. v.181 SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli Patzer,S.I.;K.Hantke
  18. FEBS Lett. v.476 Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins Pelzer,W.;U.M$\ "{u}$hlenhoff;K.Diekert;K.Siegmund;G.Kispal;R.Lill https://doi.org/10.1016/S0014-5793(00)01711-7
  19. J. Bacteriol. v.183 Genomewide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate Pomposiello,P.J.;M.H.Bennik;B.Demple https://doi.org/10.1128/JB.183.13.3890-3902.2001
  20. J. Bacteriol. v.178 Nitric oxide, Nitrite, and Fnr regulation of hmp (Flavohemoglobin) gene expression in Escherichia coli K-12 Poole,R.K.;M.F.Anjum;J.Membrillo-Hern$\ `{a}$ndez;S.O.Kim;M.N.Hughes;V.Stewart
  21. FEBS Lett. v.514 SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritima Rangachari,K.;C.T.Davis;J.F.Eccleston;E.M.A.Hirst;J.W.Saldanha;M.Strath;R.J.M.Wilson https://doi.org/10.1016/S0014-5793(02)02369-4
  22. Molecular cloning: a laboratory manual(2$2^ {nd}$ ed.) Sambrook,J.;E.F.Fritsch;T.Maniatis
  23. Experiments with gene fusions Silhavy,T.S.;M.L.Berman;L.W.Enquist
  24. Gene v.53 Improved single and multicopy lacZ-based cloning vectors for protein and operon fusions Simons,R.W.;F.Houman;N.Kleckner https://doi.org/10.1016/0378-1119(87)90095-3
  25. J. Biochem. v.126 Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli Takahashi,Y.;Nakamura,M. https://doi.org/10.1093/oxfordjournals.jbchem.a022535
  26. J. Bacteriol. v.155 Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12 Touati,D.
  27. J. Bacteriol. v.172 soxR, a locus governing a superoxide response regulon in Escherichia coli K-12 Tsaneva,I.R.;B.Weiss
  28. J. Bacteriol. v.171 Escherichia coli proteins inducible by oxidative stress mediated by the superoxide radical Walklup,L.K.;T.Kogoma
  29. J. Bacteriol. v.183 DNA Microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide Zheng,M.;X.Wang;L.J.Templeton;D.R.Smulski;R.A.Larossa;G.Storz https://doi.org/10.1128/JB.183.15.4562-4570.2001