Molecular recognition between Azotobacter vinelandii rhodanese and a sulfur acceptor protein

Biological Chemistry

Volumn 384, Issue 10-11, 2003, Pages 1473-1481

  Cereda, Angelo ^a   Forlani, Fabio ^a   Iametti, Stefania ^a   Bernhardt, Rita ^b   Ferranti, Pasquale ^c,d   Picariello, Gianluca ^d   Pagani, Silvia ^a   Bonomi, Francesco ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b SAARLAND UNIVERSITY   (Germany)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^d CNR   (Italy)

Author keywords

Adrenodoxin; Azotobacter vinelandii RhdA; Iron sulfur cluster assembly; Molecular interaction; Sulfur release; Sulfurtransferases

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; FERROUS SULFATE; SULFUR; THIOL DERIVATIVE; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; AZOTOBACTER VINELANDII; CONTROLLED STUDY; ENZYME STRUCTURE; ENZYME SUBSTRATE; FLUORESCENCE SPECTROSCOPY; MASS SPECTROMETRY; MOLECULAR RECOGNITION; MULTIGENE FAMILY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY;

ADRENODOXIN; APOPROTEINS; AZOTOBACTER VINELANDII; BINDING SITES; BLOTTING, WESTERN; CATALYTIC DOMAIN; CYSTEINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; IRON; MASS SPECTROMETRY; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL COMPOUNDS; SULFUR; SULFURTRANSFERASES; THIOSULFATE SULFURTRANSFERASE;

AZOTOBACTER; AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS); PROKARYOTA;

EID: 0344685229     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.163     Document Type: Article

References (32)

1. Beinert, H. (2000). A tribute to sulfur. Eur. J. Biochem. 267, 5657-5664.
2. Bordo, D. and Bork, P. (2002). The rhodanese/Cdc25 phosphatase superfamily. EMBO Rep. 3, 741-746.
3. Bordo, D., Deriu, D., Colnaghi, R., Carpen, A., Pagani S. and Bolognesi, M. (2000). The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between rhodanese and phosphatase enzymes family. J. Mol. Biol. 298, 691-704.
4. Bordo, D., Forlani, F., Spallarossa, A., Colnaghi, R., Carpen, A., Bolognesi, M. and Pagani, S. (2001). A persulfurated cysteine promotes active-site reactivity in Azotobacter vinelandii rhodanese. Biol. Chem. 382, 1245-1252.
5. Bradford, M.M (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principleof protein-dye binding. Anal. Biochem. 72, 248-254.
6. Colnaghi, R., Pagani, S., Kennedy, C. and Drummond, M. (1996). Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii. Eur. J. Biochem. 236, 240-248.
7. Colnaghi, R., Cassinelli, G., Drummond, M., Forlani, F. and Pagani, S. (2001). Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition. FEBS Lett. 500, 153-156.
8. Grinberg, A.V., Hanneman, F., Schiffler, B., Muller, J., Heineman, U. and Bernhardt, R. (2000). Adrenodoxin: structure, stability, and electron transfer properties. Proteins 40, 590-612.
9. Iametti, S., Bera, A.K., Vecchio, G., Grinberg, A., Bernhardt, R. and Bonomi, F. (2001). GroEL-assisted refolding of adrenodoxin during chemical cluster insertion. Eur. J. Biochem. 268, 2421-2429.
10. Kambambati, R. and Lauhon, C.T. (1999). IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry 38, 16561-16568.
11. Kambambati, R. and Lauhon, C.T. (2003). MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in E coli. Biochemistry 42, 1109-1117.
12. Kato, S., Mihara, H., Kurihara, Y., Tokumoto, U., Yoshimura, T. and Esaki, N. (2002). Cys-238 of IscS and Cys-63 of IscU are the sites of disulfide bridge 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.
13. Laemmli, U.K. (1970). Cleavage of structural proteins during the asembly of the head of bacteriophage T4. Nature 227, 680-685.
14. Marquet, A. (2001). Enzymology of carbon-sulfur bond formation. Curr. Opin. Chem. Biol. 5, 541-549.
15. Mihara, H. and Esaki, N. (2002). Bacterial cysteine desulfurases: their function and mechanism. Appl. Microbiol. Biotechnol. 60, 12-23.
16. Mueller, E.G., Palenchar, P.M. and Buck, C.J. (2001). The role of the cysteine residues of Thil in generation of 4-thiouridine in tRNA. J. Biol. Chem. 276, 33588-33595.
17. Muller, J.J., Muller, A., Rottmann, M. and Bernhardt, R. (1999). Vertebrate-type and plant-type ferredoxins: crystal structure comparison and electron transfer pathway modelling. J. Mol. Biol. 294, 501-513.
18. Nandi, L.D. and Westley, J. (1998). Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Int. J. Biochem. Cell Biol. 30, 973-977.
19. Nuth, M., Yoon, T. and Cowan, J.A. (2002). Iron-sulfur cluster biosynthesis: characterization of iron nucleation sites for assembly of the 2Fe-2S cluster core in IscU proteins. J. Am. Chem. Soc. 124, 8774-8775.
20. Ollagnier-de-Choudens, S., Mattioli, T., Takahashi, Y. and 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.
21. Pagani, S., Forlani, F., Carpen, A., Bordo, D. and Colnaghi, R. (2000). Mutagenic analysis of Thr 232 in rhodanese from Azotobacter vinelandii highlighted the differences of this prokaryotic enzyme from the known sulfurtransferases. FEBS Lett. 472, 307-311.
22. Palenchar, P.M., Buck, C.J., Cheng, H., Larson, T.J. and Mueller, E.G., (2000). Evidence that Thil, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J. Biol. Chem. 275, 8283-8286.
23. Ray, W.K., Zeng, G., Potters, M.B., Mansuri, A.M. and Larson, T.J. (2000). Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin. J. Bacteriol. 182, 2277-2284.
24. 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. 23, 11103-11104.
25. Takahashi, Y. and Nakamura, M. (1999). Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S cluster in Escherichia coli. J. Biochem. 126, 917-926.
26. Uhlmann, H., Beckert, V., Schwarz, D. and Bernhardt, R. (1992). Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of 2Fe-2S cluster ligands. Biochem. Biophys. Res. Commun. 188, 1131-1138.
27. 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.
28. Westley, J. (1977). Sulfane-transfer catalysis by enzymes. In: Bioorganic Chemistry. Vol. 1, E.E. Van Tamelen, ed. (Orlando, USA: Academic Press), pp. 371-390.
29. Williams, R.A.M., Kelly, S.M., Mottram, J.C. and Coombs G.H. (2003). 3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolism. J. Biol. Chem. 278, 1480-1486.
30. Wright, C.M., Palenchar, P.M. and Mueller, E.G. (2002). A paradigm for biological sulfur transfers via persulfide groups: a persulfide-disulfide-thiol cycle in 4-thiouridine biosynthesis. Chem. Commun. 22, 2708-2709.
31. 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.
32. 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.