Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine?

Experimental Cell Research

Volumn 316, Issue 8, 2010, Pages 1296-1303

  Arnér, Elias S J ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Cysteine; Nucleophilicity; Reactivity; Selenocysteine; Selenoprotein

Indexed keywords

CYSTEINE; SELENIUM; SELENOCYSTEINE; SELENOPROTEIN; SULFUR;

AMINO ACID SEQUENCE; CATALYSIS; CHEMICAL REACTION; ELECTRON TRANSPORT; HUMAN; MUTANT; NUCLEOPHILICITY; OXIDATION REDUCTION POTENTIAL; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN SYNTHESIS; REVIEW; ANIMAL; CHEMISTRY; GENETICS; METABOLISM;

ANIMALS; CYSTEINE; HUMANS; SELENOCYSTEINE; SELENOPROTEINS;

EID: 77952563903     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2010.02.032     Document Type: Review

References (56)

1. Yoshizawa S., Böck A. The many levels of control on bacterial selenoprotein synthesis. Biochim. Biophys. Acta 2009, 1790:1404-1414.
2. Allmang C., Wurth L., Krol A. The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated. Biochim. Biophys. Acta 2009, 1790:1415-1423.
3. Berry M.J., Martin G.W., Tujebajeva R., Grundner-Culemann E., Mansell J.B., Morozova N., Harney J.W. Selenocysteine insertion sequence element characterization and selenoprotein expression. Methods Enzymol. 2002, 347:17-24.
4. Hatfield D.L., Carlson B.A., Xu X.M., Mix H., Gladyshev V.N. Selenocysteine incorporation machinery and the role of selenoproteins in development and health. Prog. Nucleic Acid Res. Mol. Biol. 2006, 81:97-142.
5. Hatfield D.L., Gladyshev V.N. How selenium has altered our understanding of the genetic code. Mol. Cell. Biol. 2002, 22:3565-3576.
6. Driscoll D.M., Copeland P.R. Mechanism and regulation of selenoprotein synthesis. Annu. Rev. Nutr. 2003, 23:17-40.
7. Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigo R., Gladyshev V.N. Characterization of mammalian selenoproteomes. Science 2003, 300:1439-1443.
8. Kryukov G.V., Gladyshev V.N. The prokaryotic selenoproteome. EMBO Rep. 2004, 5:538-543.
9. Zhang Y., Fomenko D.E., Gladyshev V.N. The microbial selenoproteome of the Sargasso Sea. Genome Biol. 2005, 6:R37.
10. Zhang Y., Gladyshev V.N. Trends in selenium utilization in marine microbial world revealed through the analysis of the Global Ocean Sampling (GOS) project. PLoS Genet. 2008, 4:e1000095.
11. Taskov K., Chapple C., Kryukov G.V., Castellano S., Lobanov A.V., Korotkov K.V., Guigo R., Gladyshev V.N. Nematode selenoproteome: the use of the selenocysteine insertion system to decode one codon in an animal genome?. Nucleic Acids Res. 2005, 33:2227-2238.
12. Zhang Y., Romero H., Salinas G., Gladyshev V.N. Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues. Genome Biol. 2006, 7:R94.
13. Fomenko D.E., Marino S.M., Gladyshev V.N. Functional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductases. Mol. Cells 2008, 26:228-235.
14. Lobanov A.V., Hatfield D.L., Gladyshev V.N. Eukaryotic selenoproteins and selenoproteomes. Biochim. Biophys. Acta 2009, 1790:1424-1428.
15. Castellano S., Andres A.M., Bosch E., Bayes M., Guigo R., Clark A.G. Low exchangeability of selenocysteine, the 21st amino acid, in vertebrate proteins. Mol. Biol. Evol. 2009, 26:2031-2040.
16. Castellano S. On the unique function of selenocysteine-insights from the evolution of selenoproteins. Biochim. Biophys. Acta 2009, 1790:1463-1470.
17. Wessjohann L.A., Schneider A., Abbas M., Brandt W. Selenium in chemistry and biochemistry in comparison to sulfur. Biol. Chem. 2007, 388:997-1006.
18. Huber R.E., Criddle R.S. Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs. Arch. Biochem. Biophys. 1967, 122:164-173.
19. Dyson H.J., Jeng M.F., Tennant L.L., Slaby I., Lindell M., Cui D.S., Kuprin S., Holmgren A. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 1997, 36:2622-2636.
20. Kanzok S.M., Fechner A., Bauer H., Ulschmid J.K., Muller H.M., Botella-Munoz J., Schneuwly S., Schirmer R., Becker K. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science 2001, 291:643-646.
21. Gromer S., Johansson L., Bauer H., Arscott L.D., Rauch S., Ballou D.P., Williams C.H., Schirmer R.H., Arnér E.S.J. Active sites of thioredoxin reductases-why selenoproteins?. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:12618-12623.
22. Johansson L., Arscott D., Ballou D.P., Williams C.H., Arnér E.S.J. Studies of an active site mutant of the selenoprotein thioredoxin reductase: the Ser-Cys-Cys-Ser motif of the insect orhologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme. Free Radic. Biol. Med. 2006, 41:649-656.
23. Toppo S., Flohe L., Ursini F., Vanin S., Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim. Biophys. Acta 2009, 1790:1486-1500.
24. Bulaj G., Kortemme T., Goldenberg D.P. Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry 1998, 37:8965-8972.
25. Lobanov A.V., Fomenko D.E., Zhang Y., Sengupta A., Hatfield D.L., Gladyshev V.N. Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life. Genome Biol. 2007, 8:R198.
26. Bunnett J.F. Nucleophilic reactivity. Ann. Rev. Phys. Chem. 1963, 14:271-290.
27. Cedillo A., Contreras R., Galván M., Aizman A., Andrés J., Safont V.S. Nucleophilicity index from perturbed electrostatic potentials. J. Phys. Chem. A 2007, 111:2442-2447.
28. Edwards J.I., Pearson R.G. The factors determining nucleophilic reactivities. J. Am. Chem. Soc. 1962, 84:16-24.
29. Jaramillo P., Pérez P., Contreras R., Tiznado W., Fuentealba P. Definition of a nucleophilicity scale. J. Phys. Chem. A 2006, 110:8181-8187.
30. Jaramillo P., Pérez P., Fuentealba P. Relationship between basicity and nucleophilicity. J. Phys. Org. Chem. 2007, 20:1050-1057.
31. Phan T.B., Breugst M., Mayr H. Towards a general scale of nucleophilicity?. Angew. Chem. Int. Ed. 2006, 45:3869-3874.
32. Wada M., Nobuki S.-I., Tenkyuu Y., Natsume S., Asahara M., Erabi T. Bis(2,6-dimethoxyphenyl) sulfide, selenide and telluride, and their derivatives. J. Organomet. Chem. 1999, 580:282-289.
33. Pleasants J.C., Guo W., Rabenstein D.L. A comparative study of the kinetics of selenol/diselenide and thiol/disulfide exchange reactions. J. Am. Chem. Soc. 1989, 111:6553-6558.
34. Wächtershäuser G. Groundworks for an evolutionary biochemistry: the iron-sulphur world. Prog. Biophys. molec. Biol. 1992, 58:85-201.
35. Cheng Q., Sandalova T., Lindqvist Y., Arnér E.S.J. Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1. J. Biol. Chem. 2009, 284:3998-4008.
36. Arnér E.S.J. Focus on mammalian thioredoxin reductases-important selenoproteins with versatile functions. Biochim. Biophys. Acta 2009, 1790:495-526.
37. Cheng Q., Stone-Elander S., Arnér E.S.J. Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with carbon-11. Nat. Protoc. 2006, 1:604-613.
38. Cheng Q., Johansson L., Thorell J.-O., Fredriksson A., Samén E., Stone-Elander S., Arnér E.S.J. Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli. ChemBioChem 2006, 7:1976-1981.
39. Lothrop A.P., Ruggles E.L., Hondal R.J. No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue. Biochemistry 2009, 48:6213-6223.
40. Hondal R.J. Using chemical approaches to study selenoproteins-focus on thioredoxin reductases. Biochim. Biophys. Acta 2009, 1790:1501-1512.
41. Åslund F., Berndt K.D., Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 1997, 272:30780-30786.
42. Müller S., Senn H., Gsell B., Vetter W., Baron C., Böck A. The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: biosynthesis and characterization of (Se)2-thioredoxin. Biochemistry 1994, 33:3404-3412.
43. Metanis N., Keinan E., Dawson P.E. Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency. J. Am. Chem. Soc. 2006, 128:16684-16691.
44. Casi G., Roelfes G., Hilvert D. Selenoglutaredoxin as a glutathione peroxidase mimic. ChemBioChem 2008, 9:1623-1631.
45. Johansson L., Gafvelin G., Arnér E.S.J. Selenocysteine in proteins-properties and biotechnological use. Biochim. Biophys. Acta 2005, 1726:1-13.
46. Zhong L., Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J. Biol. Chem. 2000, 275:18121-18128.
47. Axley M.J., Böck A., Stadtman T.C. Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:8450-8454.
48. Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D. Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 1997, 275:1305-1308.
49. Garcin E., Vernede X., Hatchikian E.C., Volbeda A., Frey M., Fontecilla-Camps J.C. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 1999, 7:557-566.
50. Niu S., Hall M.B. Modeling the active sites in metalloenzymes 5. The heterolytic bond cleavage of H2 in the [NiFe] hydrogenase of Desulfovibrio gigas by a nucleophilic addition mechanism. Inorg. Chem. 2001, 40:6201-6203.
51. Nauser T., Dockheer S., Kissner R., Koppenol W.H. Catalysis of electron transfer by selenocysteine. Biochemistry 2006, 45:6038-6043.
52. Steinmann D., Nauser T., Beld J., Tanner M., Gunther D., Bounds P.L., Koppenol W.H. Kinetics of tyrosyl radical reduction by selenocysteine. Biochemistry 2008, 47:9602-9607.
53. May J.M., Cobb C.E., Mendiratta S., Hill K.E., Burk R.F. Reduction of the ascorbyl free radical to ascorbate by thioredoxin reductase. J. Biol. Chem. 1998, 273:23039-23045.
54. Cenas N., Nivinskas H., Anusevicius Z., Sarlauskas J., Lederer F., Arnér E.S.J. Interactions of quinones with thioredoxin reductase-a challenge to the antioxidant role of the mammalian selenoprotein. J. Biol. Chem. 2004, 279:2583-2592.
55. Cenas N., Prast S., Nivinskas H., Sarlauskas J., Arnér E.S.J. Interactions of nitroaromatic compounds with the mammalian selenoprotein thioredoxin reductase and the relation to induction of apoptosis in human cancer cells. J. Biol. Chem. 2006, 281:5593-5603.
56. Nordberg J., Zhong L., Holmgren A., Arnér E.S.J. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue. J. Biol. Chem. 1998, 273:10835-10842.