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

Journal of Biochemistry

Volumn 126, Issue 5, 1999, Pages 917-926

  Takahashi, Yasuhiro ^a   Nakamura, Minoru ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Expression; Ferredoxin; Iron sulfur cluster; Iron sulfur protein; Molecular chaperone

Indexed keywords

GENE PRODUCT; NONHEME IRON PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; ESCHERICHIA COLI; GENE CLUSTER; GENE DELETION; GENE EXPRESSION; GENE FUNCTION; GENE INACTIVATION; NONHUMAN; PLASMID; PROTEIN ASSEMBLY; REPORTER GENE;

ESCHERICHIA COLI;

EID: 0032725568     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022535     Document Type: Article

References (59)

1. Johnson, M.K. (1998) Iron-sulfur proteins: new roles for old clusters. Curr. Opin. Chem. Biol. 2, 173-181
2. Flint, D.H. and Allen, R.M. (1996) Iron-sulfur proteins with nonredox functions. Chem. Rev. 96, 2315-2334
3. Beinert, H., Kennedy, M.C., and Stout, C.D. (1996) Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem. Rev. 96, 2335-2373
4. Beinert, H., Holm, R.H., and Münck, E. (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277, 653-659
5. Sticht, H. and Rösch, P. (1998) The structure of iron-sulfur proteins. Prog. Biophys. Mol. Biol. 70, 95-136
6. Peters, J.W., Stowell, M.H.B., Soltis, S.M., Finnegan, M.G., Johnson, M.K., and Rees, D.C. (1997) Redox-dependent structural changes in the nitrogenase P-cluster. Biochemistry 36, 1181-1187
7. Peters, J.W., Lanzilotta, W.N., Lemon, B.J., and Seefeldt, L.C. (1998) X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282, 1853-1858
8. Nicolet, Y., Piras, C., Legrand, P., Hatchikian, C.E., and Fontecilla-Camps, J.C. (1999) Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure 7, 13-23
9. Crane, B.R., Siegel, L.M., and Getzoff, E.D. (1995) Sulfite reductase structure at 1.6 Å: evolution and catalysis for reduction of inorganic anions. Science 270, 59-67
10. 1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states. Biochemistry 34, 11373-11384
11. Hu, Y., Faham, S., Roy, R., Adams, M.W.W., and Rees, D.C. (1999) Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 Å resolution crystal structure and its mechanistic implications. J. Mol. Biol. 286, 899-914
12. 1 complex determined by MAD phasing at 1.5 Å resolution. Structure 4, 567-579
13. Volbeda, A., Charon, M.-H., Piras, C., Hatehikian, E.C., Frey, M., and Fontecilla-Camps, J.C. (1995) Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 373, 580-587
14. Garcin, E., Vernede, X., Hatchikian, B.C., Volbeda, A., Frey, M., and Fontecilla-Camps, J.C. (1999) The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 7, 557-566
15. Dean, D.R., Bolin, J.T., and Zheng, L. (1993) Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 175, 6737-6744
16. Zheng, L., White, R.H., Cash, V.L., Jack, R.F., and Dean, D.R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90, 2754-2758
17. Zheng, L., White, R.H., Cash, V.L., and Dean, D.R. (1994) Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry 33, 4714-4720
18. Fu, W., Jack, R.F., Morgan, T.V., Dean, D.R., and Johnson, M.K. (1994) nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 33, 13455-13463
19. Zheng, L., Cash, V.L., Flint, D.H., and Dean, D.R. (1998) Assembly of iron-sulfur clusters: identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272
20. Strain, J., Lorenz, C.R., Bode, J., Garland, S., Smolen, G.A., Ta, D.T., Vickery, L.E., and Culotta, V.C. (1998) Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. J. Biol. Chem. 273, 31138-31144
21. Nakamura, M., Saeki, K., and Takahashi, Y. (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster. J. Biochem. 126, 10-18
22. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning. A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York
23. Fujita, Y., Takahashi, Y., Chuganji, M., and Matsubara, H. (1992) The nifH-like (frxC) gene is involved in the biosynthesis of chlorophyll in the filamentous cyanobacterium Plectonema boryanum. Plant Cell Physiol. 33, 81-92
24. Miroux, B. and Walker, J.E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298
25. Blattner, F.R., Plunkett III, G., Bloch, C.A., Perna, N.T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J.D., Rode, C.K., Mayhew, G.F., Gregor, J., Davis, N.W., Kirkpatrick, H.A., Goeden, M.A., Rose, D.J., Mau, B., and Shao, Y. (1997) The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1462
26. Knoell, H.-E. and Knappe, J. (1974) Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type. Eur. J. Biochem. 50, 245-252
27. Ta, D.T. and Vickery, L.E. (1992) Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli. J. Biol. Chem. 267, 11120-11125
28. Vetter, H., Jr. and Knappe, J. (1971) Flavodoxin and ferredoxin of Escherichia coli. Hoppe-Seyler's Z. Physiol. Chem. 352, 443-446
29. Duin, E.C., Lafferty, M.E., Crouse, B.R., Allen, R.M., Sanyal, I., Flint, D.H., and Johnson, M.K. (1997) [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase. Biochemistry 36, 11811-11820
30. 2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc. Natl. Acad. Sci. USA 94, 6087-6092
31. Anderson, G.L. and Howard, J.B. (1984) Reactions with the oxidized iron protein of Azotobacter vinelandii nitrogenase: formation of a 2Fe center. Biochemistry 23, 2118-2122
32. Ryle, M.J., Lanzilotta, W.N., Seefeldt, L.C., Scarrow, R.C., and Jensen, G.M. (1996) Circular dichroism and X-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form. J. Biol. Chem. 271, 1551-1557
33. Moura, J.J.G., Moura, I., Kent, T.A., Lipscomb, J.D., Huynh, B.H., LeGall, J., Xavier, A.V., and Münck, E. (1982) Interconversions of [3Fe-3S] and [4Fe-4S] clusters. Mössbauer and electron paramagnetic resonance studies of Desulfovibrio gigas ferredoxin II. J. Biol. Chem. 257, 6259-6267
34. George, S.J., Armstrong, F.A., Hatchikian, E.C., and Thomson, A.J. (1989) Electrochemical and spectroscopic characterization of the conversion of the 7Fe into the 8Fe form of ferredoxin III from Desulfovibrio africanus. Identification of a [4Fe-4S] cluster with one non-cysteine ligand. Biochem. J. 264, 275-284
35. Conover, R.C., Kowal, A.T., Fu, W., Park, J.-B., Aono, S., Adams, M.W.W., and Johnson, M.K. (1990) Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. J. Biol. Chem. 265, 8533-8541
36. Flint, D.H. (1996) 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 dihydroxy-acid dehydratase. J. Biol. Chem. 271, 16068-16074
37. Mihara, H., Kurihara, T., Yoshimura, T., Soda, K., and Esaki, N. (1997) Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. J. Biol. Chem. 272, 22417-22424
38. Patzer, S.I. and Hantke, K. (1999) SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J Bacteriol. 181, 3307-3309
39. Howard, J.B. and Rees, D.C. (1991) Perspectives on non-heme iron protein chemistry. Adv. Protein Chem. 42, 199-280
40. Hempstead, P.D., Hudson, A.J., Artymiuk, P.J., Andrews, S.C., Banfield, M.J., Guest, J.R., and Harrison, P.M. (1994) Direct observation of the iron binding sites in a ferritin. FEBS Lett. 350, 258-262
41. Seaton, B.L. and Vickery, L.E. (1994) A gene encoding a dnaK/ hsp70 homolog in Escherichia coli. Proc. Natl. Acad. Sci. USA 91, 2066-2070
42. Silberg, J.J., Hoff, K.G., and Vickery, L.E. (1998) The Hsc66-Hsc20 chaperone system in Escherichia coli: Chaperone activity and interactions with the DnaK-DnaJ-GrpE system. J. Bacteriol. 180, 6617-6624
43. Vickery, L.E., Silberg, J.J., and Ta, D.T. (1997) Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Protein Sci. 6, 1047-1056
44. Hesterkamp, T. and Bukau, B. (1998) Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17, 4818-4828
45. Kawula, T.H. and Lelivelt, M.J. (1994) Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli. J. Bacteriol. 176, 610-619
46. Takahashi, Y., Mitsui, A., Hase, T., and Matsubara, H. (1986) Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proc. Natl. Acad. Sci. USA 83, 2434-2437
47. Takahashi, Y., Mitsui, A., and Matsubara, H. (1991) Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts. Plant Physiol. 95, 97-103
48. Takahashi, Y., Mitsui, A., Fujita, Y., and Matsubara, H. (1991) Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin. Plant Physiol. 95, 104-110
49. Ouzounis, C., Bork, P., and Sander, C. (1994) The modular structure of NifU proteins. Trends Biochem. Sci. 19, 199-200
50. Kispal, G., Csere, P., Prohl, C., and Lill, R. (1999) The mitochondrial proteins Atmlp and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981-3989
51. Matsuhisa, A., Suzuki, N., Noda, T., and Shiba, K. (1995) Inositol monophosphatase activity from the Escherichia coli suhB gene product. J. Bacteriol. 177, 200-205
52. Suzuki, H., Kim, E., Yamamoto, N., Hashimoto, W., Yamamoto, K., and Kumagai, H. (1996) Mapping, cloning, and DNA sequencing of pepB gene which encodes peptidase B of Escherichia coli K-12. J. Ferment. Bioeng. 82, 392-397
53. Fleischmann, R.D., Adams, M.D., White, O., Clayton, R.A., Kirkness, E.F., Kerlavage, A.R., Bult, C.J., Tomb, J.-F., Dougherty, B.A., Merrick, J.M., McKenney, K., Sutton, G., FitzHugh, W., Fields, C., Gocayne, J.D., Scott, J., Shirley, R., Liu, L.-I., Glodek, A., Kelley, J.M., Weidman, J.F., Phillips, C.A., Spriggs, T., Hedblom, E., Cotton, M.D., Utterback, T.R., Hanna, M.C., Nguyen, D.T., Saudek, D.M., Brandon, R.C., Fine, L.D., Fritchman, J.L., Fuhrmann, J.L., Geoghagen, N.S.M., Gnehm, C.L., McDonald, L.A., Small, K.V., Fraser, C.M., Smith, H.O., and Venter, J.C. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512
54. Barros, M.H. and Nobrega, F.G. (1999) YAH1 of Saccharomyces cerevisiae: a new essential gene that codes for a protein homologous to human adrenodoxin. Gene 233, 197-203
55. Picado-Leonard, J., Voutilainen, R., Kao, L.-C., Chung, B.-C., Strauss III, J.F., and Miller, W.L. (1988) Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. J. Biol. Chem. 263, 3240-3244
56. Mittel, S., Zhu, Y.-Z., and Vickery, L.E. (1988) Molecular cloning and sequence analysis of human placental ferredoxin. Arch. Biochem. Biophys. 264, 383-391
57. Koga, H., Yamaguchi, E., Matsunaga, K., Aramaki, H., and Horiuchi, T. (1989) Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida. J. Biochem. 106, 831-836
58. Müller, A., Müller, J.J., Muller, Y.A., Uhlmann, H., Bernhardt, R., and Heinemann, U. (1998) New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure 6, 269-280
59. Pochapsky, T.C., Jain, N.U., Kuti, M., Lyons, T.A., and Heymont, J. (1999) A refined model for the solution structure of oxidized putidaredoxin. Biochemistry 38, 4681-4690