Selenoprotein synthesis: UGA does not end the story

Biochimie

Volumn 88, Issue 11, 2006, Pages 1561-1571

  Allmang, C ^a   Krol, A ^a  

^a INST DE BIOL MOLEC ET CELLULAIRE   (France)

Author keywords

SECIS RNA protein interactions; SECp43; Selenium; Selenocysteine; Selenoproteins; SLA LP; tRNASec

Indexed keywords

SELENIUM; SELENOPROTEIN;

AMINO ACID ANALYSIS; ARTICLE; BIOSYNTHESIS; MOLECULAR DYNAMICS; SIGNAL TRANSDUCTION; STOP CODON;

MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN MODIFICATION, TRANSLATIONAL; RIBOSOMAL PROTEINS; RNA, MESSENGER; RNA, TRANSFER; RNA, TRANSFER, SER; SELENOCYSTEINE; SELENOPROTEINS;

EUKARYOTA;

EID: 33750989874     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.04.015     Document Type: Article

References (75)

1. Hatfield D.L., and Gladyshev V.N. How selenium has altered our understanding of the genetic code. Mol. Cell. Biol. 22 (2002) 3565-3576
2. Rederstorff M., Krol A., and Lescure A. Understanding the importance of selenium and selenoproteins in muscle function. Cell. Mol. Life Sci. 63 (2006) 52-59
3. Böck A. Selenium metabolism in bacteria. In: Hatfield D.L. (Ed). Selenium, its molecular biology and role in human health (2001), Kluwer Academic Publishers, Norwood, MA 7-22
4. Ser. J. Mol. Biol. 231 (1993) 274-292
5. Sec. Nucleic Acids Res. 21 (1993) 1073-1079
6. Hubert N., Sturchler C., Westhof E., Carbon P., and Krol A. The 9/4 secondary structure of eukaryotic selenocysteine tRNA: more pieces of evidence. RNA 4 (1998) 1029-1033
7. Wu X.-Q., and Gross H.J. The length and the secondary structure of the D-stem of human selenocysteine tRNA are the major identity determinants for serine phosphorylation. EMBO J. 13 (1994) 241-248
8. Böck A., Forchhammer K., Heider J., and Baron C. Selenoprotein synthesis: an expansion of the genetic code. Trends Biochem. 16 (1991) 463-467
9. [Ser]Sec. RNA 9 (2003) 923-930
10. Russell A.G., Schnare M.N., and Gray M.W. Pseudouridine-guide RNAs and other Cbf5p-associated RNAs in Euglena gracilis. RNA 10 (2004) 1034-1046
11. Shrimali R.K., Lobanov A.V., Xu X.-M., Rao M., Carlson B.A., Mahadeo D.C., Parent C.A., Gladyshev V.N., and Hatfield D.L. Selenocysteine tRNA identification in the model organisms Dictyostelium discoideum and Tetrahymena thermophila. Biochem. Biophys. Res. Com. 329 (2005) 147-151
12. Mourier T., Pain A., Barrell B., and Griffiths-Jones S. A selenocysteine tRNA and SECIS element in Plasmodium falciparum. RNA 11 (2005) 119-122
13. Leibundgut M., Frick C., Thanbichler M., Böck A., and Ban N. Selenocysteine tRNA-specific elongator factor SelB is a structural chimaera of elongation and initiation factors. EMBO J. 24 (2005) 11-22
14. Lobanov A.V., Delgado C., Rahlfs S., Novoselov S.V., Kryukov G.V., Gromer S., Hatfield D.L., Becker K., and Gladyshev V.N. The Plasmodium selenoproteome. Nucleic Acids Res. 34 (2006) 496-505
15. Sec of E.coli is the determinant for binding to elongation factors SelB or Tu. J. Biol. Chem. 266 (1991) 20375-20379
16. Sec. J. Biol. Chem. 270 (1995) 18570-18574
17. [Ser]Sec. J. Biol. Chem. 268 (1993) 14215-14223
18. Sec. Nucleic Acids Res. 22 (1994) 1354-1358
19. [Ser]Sec is governed by both primary and tertiary structure. RNA 6 (2000) 1306-1315
20. Sec complex implicated in the decoding of UGA as selenocysteine. RNA 5 (1999) 1561-1569
21. Xu X.-M., Mix H., Carlson B.A., Grabowski P.J., Gladyshev V.N., Berry M.J., and Hatfield D.L. Evidence for direct roles of two additional factors, SECp43 and Soluble Liver Antigen, in the selenoprotein synthesis machinery. J. Biol. Chem. 280 (2005) 41568-41575
22. [Ser]Sec lacking isopentenyladenosine. J. Biol. Chem. 275 (2000) 28110-28119
23. Carlson B.A., Xu X.-M., Gladyshev V.N., and Hatfield D.L. Selective rescue of selenoprotein expression in mice lacking a highly specialized methyl group in selenocysteine tRNA. J. Biol. Chem. 280 (2005) 5542-5548
24. Low S.C., Harney J.W., and Berry M.J. Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J. Biol. Chem. 270 (1995) 21659-21664
25. Guimaraes M.J., Peterson D., Vicari A., Cocks B.G., Copeland N.G., Gilbert D.J., Jenkins N.A., Ferrick D.A., Kastelein R.A., Bazan J.F., and Zlotnik A. Identification of a novel selD homolog from eukaryotes, bacteria and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?. Proc. Natl. Acad. Sci. USA 93 (1996) 15086-15091
26. Ohama T., Yang D.C.H., and Hatfield D.L. Selenocysteine tRNA and serine tRNA are aminoacylated by the same synthetase, but manifest different identities with respect to the long extra arm. Arch. Biochem. Biophys. 315 (1994) 293-301
27. Kaiser J.T., Gromadski K., Rother M., Engelhardt H., Rodnina M.V., and Wahl M.C. Structural and functional investigation of a putative archaeal selenocysteine synthase. Biochem. 44 (2005) 13315-13327
28. Gelpi C., Sontheimer E.J., and Rodriguez-Sanchez J.L. Autoantibodies against a serine tRNA-protein complex implicated in cotranslational selenocysteine insertion. Proc. Natl. Acad. Sci. USA 89 (1992) 9739-9743
29. Wies I., Brunner S., Henninger J., Herkel J., Kanzler S., Meyer zum Büschenfelde K.-H., and Lohse A.W. Identification of target antigen for SLA/LP autoantibodies in autoimmune hepatitis. Lancet 355 (2000) 1510-1515
30. [Ser]Sec complex recognized by autoantibodies from patients with type-1 autoimmune hepatitis. Clin. Exp. Immunol. 121 (2000) 364-374
31. Kernebeck T., Lohse A.W., and Grötzinger J. A bioinformatical approach suggests the function of the autoimmune hepatitis target antigen Soluble Liver Antigen/Liver Pancreas. Hepatology 34 (2001) 230-233
32. Small-Howard A., Morozova N., Stoytcheva Z., Forry E.P., Mansell J.B., Harney J.W., Carlson B.A., Xu X.-M., Hatfield D.L., and Berry M.J. Supramolecular complexes mediate selenocysteine incorporation in vivo. Mol. Cell. Biol. 26 (2006) 2337-2346
33. Tormay P., Wilting R., Lottspeich F., Mehta P.K., Christen P., and Böck A. Bacterial selenocysteine synthase, structural and functional properties. Eur. J. Biochem. 254 (1998) 655-661
34. [Ser]Sec kinase. Proc. Natl. Acad. Sci. USA 101 (2004) 12848-12853
35. Sauerwald A., Zhu W., Major T.A., Roy H., Palioura S., Jahn D., Whitman W.B., Yates III J.R., Ibba M., and Söll D. RNA-dependent cysteine biosynthesis in archaea. Science 307 (2005) 1969-1972
36. Krol A. Evolutionary different RNA motifs and RNA-protein complexes to achieve selenoprotein synthesis. Biochimie 84 (2002) 765-774
37. Driscoll D.M., and Copeland P.R. Mechanism and regulation of selenoprotein synthesis. Annu. Rev. Nutr. 23 (2003) 17-40
38. Small-Howard A.L., and Berry M.J. Unique features of selenocysteine incorporation function within the context of general eukaryotic translational processes. Biochem. Soc. 33 (2005) 1493-1497
39. Caban K., and Copeland P.R. Size matters: a view of selenocysteine incorporation from the ribosome. Cell. Mol. Life Sci. 63 (2006) 73-81
40. Walczak R., Westhof E., Carbon P., and Krol A. A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs. RNA 2 (1996) 367-379
41. Walczak R., Carbon P., and Krol A. An essential non-Watson-Crick base pair motif in 3'UTR to mediate selenoprotein translation. RNA 4 (1998) 74-84
42. Martin IV G.W., Harney J.W., and Berry M.J. Functionality of mutations at conserved nucleotides in eukaryotic SECIS elements is determined by the identity of a single nonconserved nucleotide. RNA 4 (1998) 65-73
43. nd edition, M.J.Berry, V.N.Gladyshev, D.L.Hatfield (eds), Kluwer Academic Publishers, 2006, in press.
44. Klein D.J., Schmeing T.M., Moore P.B., and Steitz T.A. The kink-turn, a new RNA secondary structure motif. EMBO J. 20 (2001) 4214-4221
45. Leontis N.B., and Westhof E. Geometric nomenclature and classification of RNA base pairs. RNA 7 (2001) 499-512
46. Grundner-Culemann E., Martin III G.W., Harney J.W., and Berry M.J. Two distinct SECIS RNA structures capable of directing selenocysteine incorporation in eukaryotes. RNA 5 (1999) 625-635
47. Fagegaltier D., Lescure A., Walczak R., Carbon P., and Krol A. Structural analysis of new local features in SECIS RNA hairpins. Nucleic Acids Res. 28 (2000) 2679-2689
48. Ramos A., Lane A.N., Hollingworth D., and Fan T.W.-N. Secondary structure and stability of the selenocysteine insertion sequences (SECIS) for human thioredoxin reductase and glutathione peroxidase. Nucleic Acids Res. 32 (2004) 1746-1755
49. Wilting R., Schorling S., Persson B.C., and Böck A. Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion. J. Mol. Biol. 266 (1997) 637-641
50. Rother M., Resch A., Gardner W.L., Whitman W.B., and Böck A. Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3' non-translated region. Mol. Microbiol. 40 (2001) 900-908
51. Kryukov G.V., and Gladyshev V.N. The prokaryotic selenoproteome. EMBO Rep. 5 (2004) 538-543
52. Copeland P.R., Fletcher J.E., Carlson B.A., Hatfield D.L., and Driscoll D.M. A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. EMBO J. 19 (2000) 306-314
53. Lescure A., Allmang C., Yamada K., Carbon P., and Krol A. cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2. Gene 291 (2002) 279-285
54. Dumitrescu A.M., Liao X.-H., Abdullah M.S.Y., Lado-Abeal J., Abdul Majed F., Moeller L.C., Boran G., Schomburg L., Weiss R.E., and Refetoff S. Mutations in SECISBP2 result in abnormal thyroid hormone metabolism. Nat. Genet. 37 (2005) 1247-1252
55. de Jesus L.A., Hoffmann P.R., Michaud T., Forry E.P., Small-Howard A., Stillwell R.J., Morozova N., Harney J.W., and Berry M.J. Nuclear assembly of UGA decoding complexes on selenoprotein mRNAs: a mechanism for eluding nonsense-mediated decay?. Mol. Cell. Biol. 26 (2006) 1795-1805
56. Allmang C., Carbon P., and Krol A. The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding. RNA 8 (2002) 1308-1318
57. Fletcher J.E., Copeland P.R., Driscoll D.M., and Krol A. The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2. RNA 7 (2001) 1442-1453
58. Allamand V., Richard P., Lescure A., Ledeuil C., Desjardin D., Petit N., Gartioux C., Ferreiro A., Krol A., Pellegrini N., Andoni Urtizberea J., and Guicheney P. A single homozygous point mutation in a 3' untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy. EMBO Rep. 7 (2006) 450-454
59. Chavatte L., Brown B.A., and Driscoll D.M. Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes. Nat. Struct. Mol. Biol. 12 (2005) 408-416
60. Halic M., Becker T., Frank J., Spahn C.M.T., and Beckmann R. Localization and dynamic behavior of ribosomal protein L30e. Nat. Struct. Mol. Biol. 12 (2005) 467-468
61. Shen Q., McQuikin P.A., and Newburger P.E. RNA-binding proteins that specifically recognize the selenocysteine insertion sequence of human cellular glutathione peroxidase mRNA. J. Biol. Chem. 270 (1995) 30448-30452
62. Hubert N., Walczak R., Carbon P., and Krol A. A protein binds the selenocysteine insertion element in the 3'UTR of mammalian selenoprotein mRNAs. Nucleic Acids Res. 24 (1996) 464-469
63. Fujiwara T., Busch K., Gross H.J., and Mizutani T. A SECIS binding protein (SBP) is distinct from selenocysteyl-tRNA protecting factor (SePF). Biochimie 81 (2000) 213-218
64. Shen Q., Wu R., Leonard J.L., and Newburger P.E. Identification and molecular cloning of a human selenocysteine insertion sequence-binding protein. A bifunctional role for DNA-binding protein B. J. Biol. Chem. 273 (1998) 5443-5446
65. Fagegaltier D., Hubert N., Carbon P., and Krol A. The selenocysteine insertion sequence binding protein SBP is different from the Y-box protein dbpB. Biochimie 82 (2000) 117-122
66. Shen Q., Fan L., and Newburger P.E. Nuclease sensitive element binding protein 1 associates with the selenocysteine insertion sequence and functions in mammalian selenoprotein translation. J. Cell. Physiol. 207 (2006) 775-783
67. Rother M., Wilting R., Commans S., and Böck A. Identification and characterization of the selenocysteine-specific translation factor SelB from the archeon Methanococcus jannaschii. J. Mol. Biol. 299 (2000) 351-358
68. Tujebajeva R.M., Copeland P.R., Xu X.-M., Carlson B.A., Harney J.W., Driscoll D.M., Hatfield D.L., and Berry M.J. Decoding apparatus for eukaryotic selenocysteine incorporation. EMBO Rep. 2 (2000) 158-163
69. Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., and Krol A. Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J. 19 (2000) 4796-4805
70. Sec-dependent assembly of the selenocysteine decoding apparatus. Mol. Cell 11 (2003) 773-781
71. Mizutani T., Tanabe K., and Yamada K. A G.U base pair in the eukaryotic selenocysteine tRNA is important for interaction with SePF, the putative selenocysteine-specific elongation factor. FEBS Lett. 429 (1998) 189-193
72. Yoshizawa S., Rasubala L., Ose T., Kohda D., Fourmy D., and Maenaka K. Structural basis for mRNA recognition by elongation factor SelB. Nat. Struct. Mol. Biol. 12 (2005) 198-203
73. Kinzy S.A., Caban K., and Copeland P.R. Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals. Nucleic Acids Res. 33 (2005) 5172-5180
74. Low S.C., Grundner-Culemann E., Harney J.W., and Berry M.J. SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy. EMBO J. 19 (2000) 6882-6890
75. Howard M.T., Aggarwal G., Anderson C.B., Khatri S., Flanigan K.M., and Atkins J.F. Recoding elements located adjacent to a subset of eukaryal selenocysteine-specifying UGA codons. EMBO J. 24 (2005) 1596-1607