Iron-sulfur cluster biosynthesis: Functional characterization of the N- and C-terminal domains of human NFU

Biochemistry

Volumn 48, Issue 5, 2009, Pages 973-980

  Liu, Yushi ^a   Qi, Wenbin ^a   Cowan, J A ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENTHALPIES; BOND CLEAVAGES; C-TERMINAL DOMAINS; CLUSTER ASSEMBLIES; COMPLEX FORMATIONS; ELECTROSTATIC INTERACTIONS; ELECTROSTATIC POTENTIAL MAPS; FUNCTIONAL CHARACTERIZATIONS; HUMAN PROTEINS; IRON-SULFUR CLUSTERS; MOLAR HEAT CAPACITIES; N- AND C- TERMINAL DOMAINS; N-TERMINAL DOMAINS; PROTEIN-PROTEIN INTERFACES; REDOX ACTIVES; REDUCTASE ACTIVITIES; SCAFFOLD PROTEINS; STRUCTURAL CHARACTERISTICS; TEMPERATURE DEPENDENCES; THIOREDOXIN;

BACTERIOLOGY; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; ELECTROSTATICS; PROTEINS; REDOX REACTIONS; SCAFFOLDS; SULFUR;

PLANTS (BOTANY);

IRON SULFUR PROTEIN; OXIDOREDUCTASE; PERSULFIDE REDUCTASE; PROTEIN NFU; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; NFU1 PROTEIN, HUMAN; NIFS PROTEIN, BACTERIA; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENTHALPY; ENZYME ACTIVITY; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; TEMPERATURE DEPENDENCE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLOGRAPHY; HUMAN; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARRIER PROTEINS; CRYSTALLOGRAPHY; HUMANS; IRON-SULFUR PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

EID: 61449125912     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801645z     Document Type: Article

References (44)

1. Beinert, H., Holm, R. H., and Munck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277, 653-659.
2. Beinert, H. (2000) Iron-sulfur proteins: Ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5, 2-15.
3. Schilke, B., Voisine, C, Beinert, H., and Craig, E. (1999) Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cereVisiae. Proc. Natl. Acad. Sci. U.S.A. 96, 10206-10211.
4. Urbina, H. D., Silberg, J. J., Hoff, K. G., and Vickery, L. E. (2001) Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly. J. Biol. Chem. 276, 44521-44526.
5. Kato, S.-I., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T., and Esaki, N. (2002) Cys-328 of IscS and Cys-63 if IscU are the sites of disulfide bridge formation in a covalent bound IscS/IscU cmoplex: Implications for the mechanism of iron-sulfur cluster assembly. Proc. Natl. Acad. Sci. U.S.A. 99, 5948-5952.
6. Frazzon, J., and Dean, D. R. (2003) Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7, 166-173.
7. Garland, S. A., Hoff, K., Vickery, L. E., and Culotta, V. C. (1999) Saccharomyces cereVisiae ISU1 and ISU2: Members of a Well-conserved Gene Family for Iron-Sulfur Cluster Assembly. J. Mol. Biol. 294, 897-907.
8. 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.
9. Kaiser, J. T., Clausen, T., Bourenkow, G. P., Bartunik, H. D., Steinbacher, S., and Huber, R. (2000) Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron sulphur cluster assembly. J. Mol. Biol. 297, 451-464.
10. Wu, S. P., Wu, G., Surerus, K. K., and 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.
11. Smith, A. D., Agar, J. N., Johnson, K A., Frazzon, J., Amster, I. J., Dean, D. R., and Johnson, M. K. (2001) Sulfur transfer from IscS to IscU: The first step in iron-sulfur cluster biosynthesis. J. Am. Chem. Soc. 123, 11103-11104.
12. 2+ cluster core in IscU proteins. J. Am. Chem. Soc. 124, 8774-8775.
13. Yoon, T, and Cowan, J. A. (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 125, 6078-6084.
14. Liu, Y., and Cowan, J. A. (2007) Iron Sulfur Cluster Biosynthesis. Human NFU Mediates Sulfide Delivery to ISU in the Final Step of [2Fe-2S] Cluster Assembly. Chem. Commun., 3192-3194.
15. Frazzon, J., Fick, J. R., and Dean, D. R. (2002) Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem. Soc. Trans. 30, 680-685.
16. Holmgren, A. (1989) Thioredoxin and Glutaredoxin Systems. J. Biol. Chem. 264, 13963-13966.
17. Yano, H, Kuroda, S., and Buchanan, R. B. (2002) Disulfide proteome in the analysis of protein function and structure. Proteomics 2, 1090-1096.
18. Ellgaard, L., and Ruddock, L. W. (2005) The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Rep. 6, 28-32.
19. Leon, S., Touraine, B., Ribot, C, Briat, J. F., and Lobreaux, S. (2003) Iron-sulphur cluster assembly in plants: Distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana. Biochem. J. 371, 823-830.
20. Tong, W. H, Jameson, G. N, Huynh, B. H., and Rouault, T. A. (2003) Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. Proc. Natl. Acad. Sci. U.S.A. 100, 9762-9767.
21. Nishio, K, and Nakai, M. (2000) Transfer of iron-sulfur cluster from NifU to apoferredoxin. J. Biol. Chem. 275, 22615-22618.
22. Lorain, S., Lecluse, Y., Scamps, C, Mattei, M. G., and Lipinski, M. (2001) Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins. Biochim. Biophys. Acta 1517, 376-383.
23. Ganesh, S., Tsurutani, N., Suzuki, T, Ueda, K, Agarwala, K. L., Osada, H, Delgado-Escueta, A. V., and Yamakawa, K (2003) The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain. Hum. Mol. Genet. 12, 2359-2368.
24. Magnaghi, P., Roberts, C, Lorain, S., Lipinski, M., and Scambler, P. J. (1998) HIRA, a mammalian homologue of Saccharomyces cereVisiae transcriptional co-repressors, interacts with Pax3. Nat. Genet. 20, 74-77.
25. Subramaniam Ganesh, N. T, Suzuki, T., Ueda, K, Lal Agarwala, K, Osada, H., Delgado-Escueta, A. V., and Yamakawa, K. (2003) The Lofora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain. Hum. Mol. Genet. 12, 2359-2368.
26. Li, K, Tong, W.-H., Hughes, R. M., and Rouault, T. A. (2006) Roles of the Mammalian Cytosolic Cysteine Desulfurase, ISCS, and Scaffold Protein, ISCU, in Iron-Sulfur Cluster Assembly. J. Biol. Chem. 281, 12344-12351.
27. Cupp-Vickery, J. R., Urbina, H., and Vickery, L. E. (2003) Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J Mol. Biol. 330, 1049-1059.
28. Percudani, R., and Peracchi, A. (2003) A genomic overview of pyridoxal-phosphate-dependent enzymes. EMBO Rep. 4, 850-854.
29. Lin, Z., Schwartz, F. P., and Eisenstein, E. (1995) The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 270, 1011-1014.
30. Murphy, K P., Privalov, P. L., and Gill, S. J. (1990) Common Feature of Protein Unfolding and Dissolution of Hydrophobic Compounds. Science 247, 559-561.
31. Manunya, N. (2004) Mechanism of Fe-S Cluster Biosynthesis: The [2Fe-2S] IscU as a Model Scaffold. Ph.D. Thesis, pp 22-26, The Ohio State University, Columbus, OH.
32. Niedzwiecka, A., Stepinski, J., Darzynkiewicz, E., Sonenberg, N., and Stolarski, R. (2002) Positive heat capacity change upon specific binding of translation initiation factor eIF4E to mRNA 5' cap. Biochemistry 41, 12140-12148.
33. Hileman, R. E., Jennings, R. N., and Linhardt, R. J. (1998) Thermodynamic analysis of the heparin interaction with a basic cyclic peptide using isothermal titration calorimetry. Biochemistry 37, 15231-15237.
34. Zhou, Y.-L., Liao, J.-M., Du, F., and Liang, Y. (2005) Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase studied by isothermal titration calorimetry and fluorescence spectroscopy. Thermochim. Acta 426, 173-178.
35. Janin, J. (1997) The kinetics of protein-protein recognition. Proteins 28, 153-161.
36. Balk, J., and Lill, R. (2004) The cell's cookbook for iron-sulfur clusters: Recipes for fool's gold? ChemBioChem 5, 1044-1049.
37. Mansy, S. S., Wu, G., Surerus, K. K., and Cowan, J. A. (2002) Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. J. Biol. Chem. 277, 21397-21404.
38. Foster, M. W., Whang, J., Penner-Hahn, J. E., Surerus, K. K., and Cowan, J. A. (2000) A mutant Human IscU Protein Contains a Stable [2Fe-2S] Center of Possible Functional Significance. J. Am. Chem. Soc. 122, 6805-6806.
39. Lorain, S., Quivy, J. P., Monier-Gavelle, F., Scamps, C, Lecluse, Y., Almouzni, G., and Lipinski, M. (1998) Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA. Mol. Cell. Biol. 18, 5546-5556.
40. Scambler, P. J. (2000) The 22q11 deletion syndromes. Hum. Mol. Genet. 9, 2421-2426.
41. Berkovic, S. F., Andermann, F., Carpenter, S., and Wolfe, L. S. (1986) Progressive myoclonus epilepsies: Specific causes and diagnosis. N. Engl. J. Med. 315, 296-305.
42. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
43. Baker, N. A, Sept, D., Joseph, S., Holst, M. J., and McCammon, J. A. (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041.
44. Pettersen, E. F., Goddard, T. D., Huang, C. C, Couch, G. S., Greenblatt, D. M., Meng, E. C, and Ferrin, T. E. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612.