Tandem use of selenocysteine: Adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase

Molecular Microbiology

Volumn 79, Issue 5, 2011, Pages 1194-1203

  Kim, Moon Jung ^a   Lee, Byung Cheon ^b,c   Jeong, Jaeho ^d   Lee, Kong Joo ^d   Hwang, Kwang Yeon ^e   Gladyshev, Vadim N ^c   Kim, Hwa Young ^a  

^a Yeungnam University College of Medicine   (South Korea)

^b UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^c BRIGHAM AND WOMEN S HOSPITAL   (United States)

^d Ewha Womans University   (South Korea)

^e Korea University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUTAREDOXIN; METHIONINE SULFOXIDE REDUCTASE; OXIDOREDUCTASE; SELENOCYSTEINE; SELENOPROTEIN; THIOL DISULFIDE OXIDOREDUCTASE; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; CLOSTRIDIUM; CONTROLLED STUDY; ESCHERICHIA COLI; GENE INSERTION SEQUENCE; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN EXPRESSION; TRANSPORT KINETICS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CLOSTRIDIUM; ESCHERICHIA COLI; GLUTAREDOXINS; KINETICS; METHIONINE SULFOXIDE REDUCTASES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN ENGINEERING; SELENOCYSTEINE; SELENOPROTEINS; SEQUENCE ALIGNMENT;

ALKALIPHILUS; BACTERIA (MICROORGANISMS); CLOSTRIDIUM; CLOSTRIDIUM SP.; ESCHERICHIA COLI;

EID: 79951808111     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07500.x     Document Type: Article

References (40)

1. Arner, E.S., Sarioglu, H., Lottspeich, F., Holmgren, A., and Bock, A. (1999) High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. J Mol Biol 292: 1003-1016.
2. Aslund, F., Berndt, K.D., and Holmgren, A. (1997) Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J Biol Chem 272: 30780-30786.
3. Bock, A., Forchhammer, K., Heider, J., Leinfelder, W., Sawers, G., Veprek, B., and Zinoni, F. (1991) Selenocysteine: the 21st amino acid. Mol Microbiol 5: 515-520.
4. Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Dorsselear, A.V., and Branlant, G. (2000) A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem 275: 35908-35913.
5. Casi, G., Roelfes, G., and Hilvert, D. (2008) Selenoglutaredoxin as a glutathione peroxidase mimic. Chembiochem 9: 1623-1631.
6. Choi, S., Jeong, J., Na, S., Lee, H.S., Kim, H.Y., Lee, K.J., and Paek, E. (2010) New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra. J Proteome Res 9: 626-635.
7. Cone, J.E., Del Rio, R.M., Davis, J.N., and Stadtman, T.C. (1976) Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety. Proc Natl Acad Sci USA 73: 2659-2663.
8. Driscoll, D.M., and Copeland, P.R. (2003) Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr 23: 17-40.
9. Fourmy, D., Guittet, E., and Yoshizawa, S. (2002) Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB. J Mol Biol 324: 137-150.
10. Ge, Y., Qi, Z., Wang, Y., Liu, X., Li, J., Xu, J., etal. (2009) Engineered selenium-containing glutaredoxin displays strong glutathione peroxidase activity rivaling natural enzyme. Int J Biochem Cell Biol 41: 900-906.
11. Gladyshev, V.N., Jeang, K.T., and Stadtman, T.C. (1996) Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci USA 93: 6146-6151.
12. Gromer, S., Johansson, L., Bauer, H., Arscott, L.D., Rauch, S., Ballou, D.P., etal. (2003) Active sites of thioredoxin reductases: why selenoproteins? Proc Natl Acad Sci USA 100: 12618-12623.
13. Hatfield, D.L., and Gladyshev, V.N. (2002) How selenium has altered our understanding of the genetic code. Mol Cell Biol 22: 3565-3576.
14. Holmgren, A. (1976) Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci USA 73: 2275-2279.
15. Holmgren, A., Johansson, C., Berndt, C., Lonn, M.E., Hudemann, C., and Lillig, C.H. (2005) Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans 33: 1375-1377.
16. Hondal, R.J., and Ruggles, E.L. (2010) Differing views of the role of selenium in thioredoxin reductase. Amino Acids doi:10.1007/s00726-010-0494-6.
17. Kim, H.Y., and Gladyshev, V.N. (2004) Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 15: 1055-1064.
18. Kim, H.Y., and Gladyshev, V.N. (2005) Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases. PLoS Biol 3: e375.
19. Kim, H.Y., and Gladyshev, V.N. (2007) Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 407: 321-329.
20. Kim, H.Y., Fomenko, D.E., Yoon, Y.E., and Gladyshev, V.N. (2006) Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochem 45: 13697-13704.
21. Kim, H.Y., Zhang, Y., Lee, B.C., Kim, J.R., and Gladyshev, V.N. (2009) The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A. Proteins 74: 1008-1017.
22. Kumar, R.A., Koc, A., Cerny, R.L., and Gladyshev, V.N. (2002) Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J Biol Chem 277: 37527-37535.
23. Lee, S.R., Bar-Noy, S., Kwon, J., Levine, R.L., Stadtman, T.C., and Rhee, S.G. (2000) Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proc Natl Acad Sci USA 97: 2521-2526.
24. Lillig, C.H., and Holmgren, A. (2007) Thioredoxin and related molecules - from biology to health and disease. Antioxid Redox Signal 9: 25-47.
25. Lillig, C.H., Berndt, C., and Holmgren, A. (2008) Glutaredoxin systems. Biochim Biophys Acta 1780: 1304-1317.
26. Liu, Z., Reches, M., Groisman, I., and Engelberg-Kulka, H. (1998) The nature of the minimal 'selenocysteine insertion sequence' (SECIS) in Escherichia coli. Nucleic Acids Res 26: 896-902.
27. Lowther, W.T., Brot, N., Weissbach, H., and Matthews, B.W. (2000) Structure and mechanism of peptide methionine sulfoxide reductase, an 'anti-oxidation' enzyme. Biochem 39: 13307-13312.
28. Metanis, N., Keinan, E., and Dawson, P.E. (2006) Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J Am Chem Soc 128: 16684-16691.
29. Regeimbal, J., and Bardwell, J.C. (2002) DsbB catalyzes disulfide bond formation de novo. J Biol Chem 277: 32706-32713.
30. Sambol, A.R., and Dubes, G.R. (1984) Phenotypic suppression of opal mutants by L-tryptophan. Microbios 39: 19-27.
31. Sandman, K.E., and Noren, C.J. (2000) The efficiency of Escherichia coli selenocysteine insertion is influenced by the immediate downstream nucleotide. Nucleic Acids Res 28: 755-761.
32. Sandman, K.E., Tardiff, D.F., Neely, L.A., and Noren, C.J. (2003) Revised Escherichia coli selenocysteine insertion requirements determined by in vivo screening of combinatorial libraries of SECIS variants. Nucleic Acids Res 31: 2234-2241.
33. Schuster, P., Fontana, W., Stadler, P.F., and Hofacker, I.L. (1994) From sequences to shapes and back: a case study in RNA secondary structures. Proc Biol Sci 255: 279-284.
34. Stadtman, T.C. (1996) Selenocysteine. Annu Rev Biochem 65: 83-100.
35. Su, D., and Gladyshev, V.N. (2004) Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1. Biochem 43: 12177-12188.
36. Su, D., Li, Y., and Gladyshev, V.N. (2005) Selenocysteine insertion directed by the 3'-UTR SECIS element in Escherichia coli. Nucleic Acids Res 33: 2486-2492.
37. Tete-Favier, F., Cobessi, D., Boschi-Muller, S., Azza, S., Branlant, G., and Aubry, A. (2000) Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Structure 8: 1167-1178.
38. Tormay, P., and Bock, A. (1997) Barriers to heterologous expression of a selenoprotein gene in bacteria. J Bacteriol 179: 576-582.
39. Zhang, Y., and Gladyshev, V.N. (2005) An algorithm for identification of bacterial selenocysteine insertion sequence elements and selenoprotein genes. Bioinformatics 21: 2580-2589.
40. Zhang, Y., Romero, H., Salinas, G., and Gladyshev, V.N. (2006) Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues. Genome Biol 7: R94.