A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis

Journal of Biological Chemistry

Volumn 283, Issue 37, 2008, Pages 25178-25185

  Marelja, Zvonimir ^a   Stöcklein, Walter ^a   Nimtz, Manfred ^b   Leimkühler, Silke ^a  

^a UNIVERSITY OF POTSDAM   (Germany)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; CYTOLOGY; ENZYMES; ESCHERICHIA COLI; MOLYBDENUM; PLASMA JETS; PURIFICATION;

ADENYLATION; C TERMINUSES; COFACTOR; CYSTEINE DESULFURASE; CYTOSOL; CYTOSOLIC; DITHIOLENE; DO-MAINS; HETEROLOGOUS EXPRESSION SYSTEMS; IN-VIVO; MOLYBDOPTERIN; MUTAGENESIS STUDIES; PROTEIN INTERACTIONS; PURIFIED PROTEINS; SULFUR DONORS; SULFUR SOURCES; SULFUR TRANSFERS; SYNTHASE;

SULFUR;

CYSTEINE; L CYSTEINE DESULFURASE; MOLYBDENUM; PERSULFIDE; SULFIDE; SULFURTRANSFERASE; UNCLASSIFIED DRUG; CYSTATHIONINE GAMMA LYASE; LYASE; METALLOPROTEIN; MOCS3 PROTEIN, HUMAN; MOLYBDENUM COFACTOR; NFS1 PROTEIN, HUMAN; NUCLEOTIDYLTRANSFERASE; PTERIDINE DERIVATIVE; SULFUR; THIOSULFATE;

ARTICLE; CONTROLLED STUDY; CYTOPLASM; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE; GENE EXPRESSION SYSTEM; KINETICS; MOCS3 GENE; NFS1 GENE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; PROTEIN PURIFICATION; BIOLOGICAL MODEL; BIOSYNTHESIS; CATALYSIS; CHEMISTRY; COENZYME; GENE EXPRESSION REGULATION; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SURFACE PLASMON RESONANCE;

ESCHERICHIA COLI; EUKARYOTA;

CARBON-SULFUR LYASES; CATALYSIS; COENZYMES; CYTOPLASM; GENE EXPRESSION REGULATION; HUMANS; KINETICS; METALLOPROTEINS; MODELS, BIOLOGICAL; NUCLEOTIDYLTRANSFERASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PTERIDINES; SULFUR; SULFURTRANSFERASES; SURFACE PLASMON RESONANCE; THIOSULFATES;

EID: 54449085541     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804064200     Document Type: Article

References (49)

1. Marquet, A. (2001) Curr. Opin. Chem. Biol. 5, 541-549
2. Rajagopalan, K. V., Johnson, J. L., and Hainline, B. E. (1982) Fed. Proc. 41, 2608-2612
3. Johnson, J. L., and Duran, M. (2001) in The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S., Valle, D., Childs, B., and Vogelstein, B., eds), pp. 3163-3177, 8th edition, McGraw-Hill, New York
4. Rajagopalan, K. V. (1996) in Escherichia coli and Salmonella. Cellular and Molecular Biology (Neidhardt, F. C., ed), pp. 674-679, ASM Press, Washington, DC
5. Reiss, J. (2000) Hum. Genet 106, 157-163
6. Leimkühler, S., Freuer, A., Santamaria Araujo, J. A., Rajagopalan, K. V., and Mendel, R. R. (2003) J. Biol. Chem. 278, 26127-26134
7. Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V., and Schindelin, H. (2001) Nature 414, 325-329
8. Leimkühler, S., and Rajagopalan, K. V. (2001) J. Biol. Chem. 276, 22024-22031
9. Leimkühler, S., Wuebbens, M. M., and Rajagopalan, K. V. (2001) J. Biol. Chem. 276, 34695-34701
10. Wuebbens, M. M., and Rajagopalan, K. V. (2003) J. Biol. Chem. 278, 14523-14532
11. Schmitz, J., Mullich Cowdhury, M., Hänzelmann, P., Lee, E.-Y., Schindelin, H., and Leimkühler, S. (2008) Biochemistry 47, 4679-4689
12. Krepinsky, K., and Leimkühler, S. (2007) FEBS J. 274, 2778-2787
13. Matthies, A., Nimtz, M., and Leimkühler, S. (2005) Biochemistry 44, 7912-7920
14. Matthies, A., Rajagopalan, K. V., Mendel, R. R., and Leimkühler, S. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 5946-5951
15. Bordo, D., and Bork, P. (2002) Embo. Reports 3, 741-746
16. Mueller, E. G. (2006) Nat. Chem. Biol. 2, 185-194
17. Zheng, L., White, R. H., Cash, V. L., Jack, R. F., and Dean, D. R. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 2754-2758
18. Mihara, H., and Esaki, N. (2002) Appl. Microbiol. Biotechnol. 60, 12-23
19. Land, T., and Rouault, T. A. (1998) Mol. Cell 2, 807-815
20. Biederbick, A., Stehling, O., Rosser, R., Niggemeyer, B., Nakai, Y., Elsasser, H. P., and Lill, R. (2006) Mol. Cell Biol. 26, 5675-5687
21. Li, K., Tong, W. H., Hughes, R. M., and Rouault, T. A. (2006) J. Biol. Chem. 281, 12344-12351
22. Tong, W. H., and Rouault, T. (2000) EMBO J. 19, 5692-5700
23. Tong, W. H., and Rouault, T. A. (2006) Cell Metab. 3, 199-210
24. Adam, A. C., Bornhovd, C., Prokisch, H., Neupert, W., and Hell, K. (2006) EMBO J. 25, 174-183
25. Wiedemann, N., Urzica, E., Guiard, B., Müller, H., Lohaus, C., Meyer, H. E., Ryan, M. T., Meisinger, C., Mühlenhoff, U., Lill, R., and Pfanner, N. (2006) EMBO J. 25, 184-195
26. Shan, Y., Napoli, E., and Cortopassi, G. (2007) Hum. Mol. Genet 16, 929-941
27. Richards, T. A., and van der Giezen, M. (2006) Mol. Biol. Evol. 23, 1341-1344
28. Fogo, J. K., and Popowsky, M. (1949) Anal Chem. 21, 732-734
29. Urbina, H. D., Silberg, J. J., Hoff, K. G., and Vickery, L. E. (2001) J. Biol. Chem. 276, 44521-44526
30. Peterson, E. A., and Sober, H. A. (1954) J. Am. Chem. Soc. 76, 169-175
31. Neumann, M., Schulte, M., Jünemann, N., Stöcklein, W., and Leimkühler, S. (2006) J. Biol. Chem. 281, 15701-15708
32. Sörbo, B. (1957) Biochim. Biophys. Acta 23, 412-416
33. Lauhon, C. T., and Kambampati, R. (2000) J. Biol. Chem. 275, 20096-20103
34. Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Biochemistry 33, 4714-4720
35. Zheng, L., Cash, V. L., Flint, D. H., and Dean, D. R. (1998) J. Biol. Chem. 273, 13264-13272
36. Takahashi, Y., and Tokumoto, U. (2002) J. Biol. Chem. 277, 28380-28383
37. Outten, F. W., Djaman, O., and Storz, G. (2004) Mol. Microbiol. 52, 861-872
38. Loiseau, L., Ollagnier-de Choudens, S., Lascoux, D., Forest, E., Fontecave, M., and Barras, F. (2005) J. Biol. Chem. 280, 26760-26769
39. Frazzon, J., and Dean, D. R. (2003) Curr. Opin. Chem. Biol. 7, 166-173
40. Lill, R., and Mühlenhoff, U. (2008) Annu. Rev. Biochem. 77, 669-700
41. Lill, R., and Mühlenhoff, U. (2006) Annu. Rev. Cell Dev. Biol. 22, 457-486
42. Nakai, Y., Nakai, M., Lill, R., Suzuki, T., and Hayashi, H. (2007) Mol. Cell Biol. 27, 2841-2847
43. Lill, R., Dutkiewicz, R., Elsasser, H. P., Hausmann, A., Netz, D. J., Pierik, A. J., Stehling, O., Urzica, E., and Mühlenhoff, U. (2006) Biochim. Biophys. Acta 1763, 652-667
44. Rouault, T. A., and Tong, W. H. (2005) Nat. Rev. Mol. Cell Biol. 6, 345-351
45. Mühlenhoff, U., Balk, J., Richhardt, N., Kaiser, J. T., Sipos, K., Kispal, G., and Lill, R. (2004) J. Biol. Chem. 279, 36906-36915
46. Hille, R. (1996) Chemical Rev. 96, 2757-2816
47. Reiss, J., and Johnson, J. L. (2003) Hum. Mutat. 21, 569-576
48. Duran, M., de Bree, P. K., de Klerk, J. B. C., Dorland, L., and Berger, R. (1996) Int. Pediatr. 11, 334-338
49. Zhang, Y., and Gladyshev, V. N. (2008) J. Mol. Biol. 379, 881-899