Asp97 is a Crucial Residue Involved in the Ligation of the [] Cluster of IscA from Acidithiobacillus ferrooxidans |
Jiang, Huidan
(Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University)
Zhang, Xiaojian (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) Ai, Chenbing (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) Liu, Yuandong (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) Liu, Jianshe (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) Qiu, Guanahou (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) Zeng, Jia (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) |
1 | Agar, J. N., C. Krebs, J. Frazzon, B. H. Huynh, D. R. Dean, and M. K. Johnson. 2000. IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe- 4S] clusters in IscU. Biochemistry 39: 7856-7862 DOI ScienceOn |
2 | Caspersen, M. B., K. Bennett, and H. E. Christensen. 2000. Expression and characterization of recombinant Rhodocyclus tenuis high potential iron-sulfur protein. Protein Expr. Purif. 19: 259-264 DOI ScienceOn |
3 | Cavazza, C., B. Guigliarelli, P. Bertrand, and M. Bruschi. 1995. Biochemical and EPR characterization of a high potential ironsulfur protein in Thiobacillus ferrooxidans. FEMS Microbiol. Lett. 130: 193-200 DOI |
4 | Davidson, E., T. Ohnishi, E. Atta-Asafo-Adjei, and F. Daldal. 1992. Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of Rhodobacter capsulatus probed by site-directed mutagenesis. Biochemistry 31: 3342-3351 DOI ScienceOn |
5 | Kerfeld, C. A., A. E. Salmeen, and T. O. Yeates. 1998. Crystal structure and possible dimerization of the high-potential ironsulfur protein from Chromatium purpuratum. Biochemistry 37: 13911-13917 DOI ScienceOn |
6 | Kurihara, T., H. Mihara, S. Kato, T. Yoshimura, and N. Esaki. 2003. Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD from Escherichia coli. Biochim. Biophys. Acta 1647: 303-309 DOI ScienceOn |
7 | Mansy, S. S., G. Wu, K. K. Surerus, and J. A. Cowan. 2002. Iron-sulfur cluster biosynthesis: Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. J. Biol. Chem. 277: 21397-21404 DOI ScienceOn |
8 | Schwartz, C. J., O. Djaman, J. A. Imlay, and P. J. Kiley. 2000. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl. Acad. Sci. USA 97: 9009-9014 |
9 | Smith, A. D., J. N. Agar, K. A. Johnson, J. Frazzon, I. J. Amster, D. R. Dean, and M. K. Johnson. 2001. Sulfur transfer from IscS to IscU: The first step in iron-sulfur cluster biosynthesis. J. Am. Chem. Soc. 123: 11103-11104 DOI ScienceOn |
10 | Thompson, J., T. Gibson, F. Plewniak, F. Jeanmougin, and D. Higgins. 1997. The CLUSTAL_X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 24: 4876-4882 |
11 | Urbina, H. D., J. J. Silberg, K. G. Hoff, and L. E. Vickery. 2001. Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. J. Biol. Chem. 276: 44521-44526 DOI ScienceOn |
12 | Wu, G., S. S. Mansy, C. Hemann, R. Hille, K. K. Surerus, and J. A. Cowan. 2002. Iron-sulfur cluster biosynthesis: Characterization of Schizosaccharomyces pombe Isa1. J. Biol. Inorg. Chem. 7: 526-532 DOI ScienceOn |
13 | Zheng, L., L. Cash, D. H. Flint, and D. R. Dean. 1998. Assembly of iron-sulfur clusters. Identification of an iscSUAhscBA- fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273: 13264-13272 DOI ScienceOn |
14 | Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680- 685 DOI ScienceOn |
15 | Tokumoto, U. and Y. Takahashi. 2001. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. (Tokyo) 130: 63-71 DOI ScienceOn |
16 | Ollagnier-de-Choudens, S., T. Mattioli, Y. Takahashi, and M. Fontecave. 2001. Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 276: 22604-22607 DOI ScienceOn |
17 | Kaut, A., H. Lange, K. Diekert, G. Kispal, and R. Lill. 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 DOI ScienceOn |
18 | Bruscella, P., L. Cassagnaud, J. Ratouchniak, G. Brasseur, E. Lojou, R. Amils, and V. Bonnefoy. 2005. The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms. Microbiology 151: 1421-1431 DOI ScienceOn |
19 | Bilder, P., H. Ding, and M. Newcomer. 2004. The crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry 43: 133-139 DOI ScienceOn |
20 | Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254 DOI ScienceOn |
21 | Nishio, K. and M. Nakai. 2000. Transfer of iron-sulfur cluster from NifU to apoferredoxin. J. Biol. Chem. 275: 22615-22618 DOI ScienceOn |
22 | Krebs, C., J. N. Agar, A. D. Smith, J. Frazzon, D. R. Dean, B. H. Huynh, and M. K. Johnson. 2001. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry 40: 14069-14080 DOI ScienceOn |
23 | Siegel, L. M. 1965. A direct microdetermination for sulfide. Anal. Biochem. 11: 126-132 DOI ScienceOn |
24 | Tokumoto, U., S. Nomura, Y. Minami, H. Mihara, S. Kato, T. Kurihara, N. Esaki, H. Kanazawa, H. Matsubara, and Y. Takahashi. 2002. Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. J. Biochem. (Tokyo) 131: 713-719 DOI ScienceOn |
25 | Cupp-Vickery, J. R., J. J. Silberg, D. T. Ta, and L. E. Vickery. 2004. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. J. Mol. Biol. 338: 127-137 DOI ScienceOn |
26 | Rees, D. C. and J. B. Howard. 2003. The interface between the biological and inorganic worlds: Iron-sulfur metalloclusters. Science 300: 929-931 DOI |
27 | Morimoto, K., E. Yamashita, Y. Kondou, S. J. Lee, F. Arisaka, T. Tsukihara, and M. Nakai. 2006. The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold. J. Mol. Biol. 360: 117-132 DOI ScienceOn |
28 | Zeng, J., M. Geng, H. Jiang, Y. Liu, J. Liu, and G. Qiu. 2007. The Isc A from Acidithiobacillus ferrooxidans is an iron-sulfur protein which assembles the [Fe4S4] cluster with intracellular iron and sulfur. Arch. Biochem. Biophys. 463: 237-244 DOI ScienceOn |
29 | Kiley, P. J. and H. Beinert. 2003. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6: 181-185 DOI ScienceOn |
30 | Johnson, M. K. 1998. Iron-sulfur proteins: New roles for old clusters. Curr. Opin. Chem. Biol. 2: 173-181 DOI ScienceOn |
31 | Nogi, T., I. Fathir, M. Kobayashi, T. Nozawa, and K. Miki. 2000. Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer. Proc. Natl. Acad. Sci. USA 97: 13561-13566 |
32 | Wollenberg, M., C. Berndt, E. Bill, J. D. Schwenn, and A. Seidler. 2003. A dimer of the FeS cluster biosynthesis protein IscA from Cyanobacteria binds a [2Fe-2S] cluster between two protomers and transfers it to [2Fe-2S] and [4Fe-4S] apo proteins. Eur. J. Biochem. 270: 1662-1671 DOI ScienceOn |
33 | Beinert, H., R. H. Holm, and E. Munck. 1997. Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277: 653-659 DOI |
34 | Takahashi, Y. and M. Nakamura. 1999. Functional assignment of the ORF2-iscSiscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J. Biochem. (Tokyo) 126: 917-926 DOI ScienceOn |
35 | Liu, J., N. Oganesyan, D. H. Shin, J. Jancarik, H. Yokota, R. Kim, and S. H. Kim. 2005. Structural characterization of an iron-sulfur cluster assembly protein IscU in a zinc-bound form. Proteins 59: 875-881 DOI ScienceOn |
36 | Lovenberg, W., B. B. Buchanan, and J. C. Rabinowitz. 1963. Studies on the chemical nature of clostridial ferredoxin. J. Biol. Chem. 238: 3899-3913 |
37 | Ding, H. and R. J. Clark. 2004. Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem. J. 379: 433-440 DOI ScienceOn |
38 | Yang, W., P. A. Rogers, and H. Ding. 2002. Repair of nitric oxide modified ferredoxin [2Fe-2S] cluster by cysteine desulfurase (IscS). J. Biol. Chem. 277: 12868-12873 DOI ScienceOn |