A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins

European Journal of Biochemistry

Volumn 270, Issue 8, 2003, Pages 1662-1671

  Wollenberg, Markus ^a   Berndt, Carsten ^a   Bill, Eckhard ^b   Schwenn, Jens D ^a   Seidler, Andreas ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

Author keywords

Assembly; Cofactor; Iron sulfur cluster; IscA; Synechocystis

Indexed keywords

ADENOSINE 5' PHOSPHOSULFATE; CYSTEINE; DIMER; FERREDOXIN; IRON; IRON SULFUR PROTEIN; PROTEIN; PROTEIN ISCA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; CONTROLLED STUDY; CYANOBACTERIUM; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; INCUBATION TIME; MOSSBAUER SPECTROSCOPY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; APOPROTEINS; BACTERIAL PROTEINS; CONSERVED SEQUENCE; CYANOBACTERIA; IRON-SULFUR PROTEINS; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OPEN READING FRAMES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTROSCOPY, MOSSBAUER;

BACTERIA (MICROORGANISMS); CYANOBACTERIA; ESCHERICHIA COLI; NEGIBACTERIA; SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 0038409882     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03522.x     Document Type: Article

References (36)

1. Beinert, H. (2000) Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5, 2-15.
2. Jacobson, M.R., Cash, V.L., Weiss, M.C., Laird, N.F., Newton, W.E. & Dean, D.R. (1989) Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. Mol. Gen. Genet. 219, 49-57.
3. Lill, R. & Kispal, G. (2000) Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends. Biochem. Sci. 25, 352-358.
4. Zheng, L., Cash, V.L., Flint, D.H. & Dean, D.R. (1998) Assembly of Iron-sulfur Clusters. J. Biol. Chem. 273, 13264-13272.
5. Zheng, L., White, R.H., Cash, V.L., Jack, R.F. & Dean, D.R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl Acad. Sci. USA 90, 2754-2758.
6. Yuvaniyama, P., Agar, J.N., Cash, V.L., Johnson, M.K. & Dean, D.R. (2000) NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proc. Natl Acad. Sci. USA 97, 599-604.
7. Agar, J.N., Zheng, L., Cash, V.L., Dean, D.R. & Johnson, M.K. (2000) Role of the IscU protein in iron-sulfur cluster biosynthesis: IscS-mediated assembly of a (Fe2S2) Cluster in IscU. J. Am. Chem. Soc. 122, 2137-2137.
8. Urbina, H.D., Silberg, J.J., Hoff, K.G. & Vickery, L.E. (2001) Transfer of sulfur from IscS to IscU during FeS cluster assembly. J. Biol. Chem. 276, 44521-44526.
9. Kato, S., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T. & Esaki, N. (2002) Cys328 of IscS and Cys63 of IscU are sites of disulfide brdige formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly. Proc. Natl Acad. Sci. USA 99, 5948-5952.
10. Agar, J.N., Krebs, C., Frazzon, J., Huynh, B.H., Dean, D.R. & Johnson, M.K. (2000) IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in NifU. Biochemistry 39, 7856-7862.
11. 2+ center of possible functional significans. J. Am. Chem. Soc. 122, 6805-6806.
12. Wu, S.P., Wu, G., Surerus, K.K. & Cowan, J.A. (2002) Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate. Biochemistry 41, 8876-8885.
13. Hoff, KG., Silberg, J.J. & Vickery, L.E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc. Natl Acad. Sci. USA 97, 7790-7795.
14. Silberg, J.J., Hoff, K.G., Tapley, T.L. & Vickery, L.E. (2001) The FeS assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 276, 1696-1700.
15. ISVW gene region: possible role of NifW in homocitrate processing. Mol. Gen. Genet. 238, 369-382.
16. Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., Miyajima, N., Hirosawa, M., Sugiura, M., Sasamoto, S., Kimura, T., Hosouchi, T., Matsuno, A., Muraki, A., Nakazaki, N., Naruo, K., Okumura, S., Shimpo, S., Takeuchi, C., Wada, T. & Watanabe, A. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3, 109-136.
17. Seidler, A., Jaschkowitz, K. & Wollenberg, M. (2001) Incorporation of iron-sulphur clusters in membrane-bound proteins. Biochem. Soc. Trans. 29, 418-421.
18. 1fdx-ORF3 gone cluster involved in the assembly of FeS clusters in Escherichia coli. J. Biochem. 126, 917-926.
19. Tokumoto, U. & Takahashi, Y. (2001) genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. 130, 63-71.
20. Kaut, A., Lange, H., Diekert, K., Kispal, G. & Lill, R. (2000) Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function. J. Biol. Chem. 275, 15955-15961.
21. Jensen, L.T. & Culotta, V.C. (2000) Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell Biol. 20, 3918-3927.
22. Pelzer, W., Mühlenhoff, U., Diekert, K., Siegmund, K., Lispal, G. & Lill, R. (2000) Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins. FEBS Lett. 476, 134-139.
23. Schöpfer, R. (1993) The pRSET family of T7 promoter expression vectors for Escherichia coli. Gene 124, 83-85.
24. Kunkel, T.A., Roberts, J.D. & Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
25. Jaschkowitz, K. & Seidler, A. (2000) The role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins. Biochemistry 39, 3416-3423.
26. Barth, P., Guillard, I., Setif, P. & Lagoutte, B. (2000) Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin. J. Biol. Chem. 275, 7030-7036.
27. Prior, A., Uhrig, J.F., Heins, L., Wiesmann, A., Lillig, C.H., StoNe, C., Soll, J. & Schwenn, J.D. (1999) Structural and kinetic properties of adenylyl sulfate reductase from Catharantus roseus cell cultures. Biochim. Biophys. Acta. 1430, 25-38.
28. Meyer, J., Moulis, J. & Lutz, M. (1986) High-yield chemical assembly of 2Fe-2X (X = S, Se) clusters into spinach apoferredoxin: product characterization by resonance Raman spectroscopy. Biochim. Biophys. Acta 871, 243-249.
29. Schwenn, J.D. & Schriek, U. (1987) PAPS-reductase from Escherichia coli: characterization of the enzyme as probe for thioredoxins. Z. Naturforsch. 42c, 93-102.
30. Siegel, L.M. (1965) A direct microdetermination for sulfide. Anal. Biochem. 11, 126-132.
31. Fish, W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 158, 357-364.
32. Seidler, A. (1994) Expression of the 23 kDa protein from the oxygen-evolving complex of higher plants in Escherichia coli. Biochim. Biophys. Acta. 1187, 73-79.
33. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
34. Ollagnier-de-Choudens, S., Mattioli, T., Takahashi, Y. & Fontecave, M. (2001) Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 276, 22604-22607.
35. Krebs, C., Agar, J.N., Smith, A.D., Frazzon, J., Dean, D.R., Huynh, B.H. & Johnson, M.K. (2001) IscA, an alternate scaffold for the FeS cluster biosynthesis. Biochemistry 40, 14069-14080.
36. 2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc. Natl Acad. Sci. USA 94, 6087-6092.