Identification of a signature motif for the eIF4a3-SECIS interaction

Nucleic Acids Research

Volumn 39, Issue 17, 2011, Pages 7730-7739

  Budiman, Michael E ^a   Bubenik, Jodi L ^a   Driscoll, Donna M ^a,b  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4A; INITIATION FACTOR 4A3; SELENOCYSTEINE; UNCLASSIFIED DRUG; URIDINE;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; GENE INSERTION SEQUENCE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOOTPRINTING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SELENOCYSTEINE INSERTION SEQUENCE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SURFACE PLASMON RESONANCE;

3' UNTRANSLATED REGIONS; ANIMALS; BINDING SITES; DEAD-BOX RNA HELICASES; NUCLEIC ACID CONFORMATION; PEPTIDE INITIATION FACTORS; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, TERTIARY; RATS; RNA, MESSENGER; SELENOPROTEINS; URIDINE;

EID: 80053204231     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr446     Document Type: Article

References (45)

1. Li, Q., Imataka, H., Morino, S., Rogers, G.W. Jr, Richter-Cook, N.J., Merrick, W.C. and Sonenberg, N. (1999) Eukaryotic translation initiation factor 4AIII (eIF4AIII) is functionally distinct from eIF4AI and eIF4AII. Mol. Cell. Biol., 19, 7336-7346. (Pubitemid 29493397)
2. Chan, C.C., Dostie, J., Diem, M.D., Feng, W., Mann, M., Rappsilber, J. and Dreyfuss, G. (2004) eIF4A3 is a novel component of the exon junction complex. RNA, 10, 200-209. (Pubitemid 38129825)
3. Shibuya, T., Tange, T.O., Sonenberg, N. and Moore, M.J. (2004) eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay. Nat. Struct. Mol. Biol., 11, 346-351. (Pubitemid 38436799)
4. Palacios, I.M., Gatfield, D., St Johnston, D. and Izaurralde, E. (2004) An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay. Nature, 427, 753-757. (Pubitemid 38294596)
5. Ferraiuolo, M.A., Lee, C.S., Ler, L.W., Hsu, J.L., Costa-Mattioli, M., Luo, M.J., Reed, R. and Sonenberg, N. (2004) A nuclear translation-like factor eIF4AIII is recruited to the mRNA during splicing and functions in nonsense-mediated decay. Proc. Natl Acad. Sci. USA, 101, 4118-4123. (Pubitemid 38405893)
6. Tange, T.O., Nott, A. and Moore, M.J. (2004) The ever-increasing complexities of the exon junction complex. Curr. Opin. Cell Biol., 16, 279-284. (Pubitemid 38610408)
7. Bono, F., Ebert, J., Lorentzen, E. and Conti, E. (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell, 126, 713-725. (Pubitemid 44233638)
8. Andersen, C.B., Ballut, L., Johansen, J.S., Chamieh, H., Nielsen, K.H., Oliveira, C.L., Pedersen, J.S., Seraphin, B., Le Hir, H. and Andersen, G.R. (2006) Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. Science, 313, 1968-1972. (Pubitemid 44498005)
9. Ballut, L., Marchadier, B., Baguet, A., Tomasetto, C., Seraphin, B. and Le Hir, H. (2005) The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. Nat. Struct. Mol. Biol., 12, 861-869. (Pubitemid 41486709)
10. Budiman, M.E., Bubenik, J.L., Miniard, A.C., Middleton, L.M., Gerber, C.A., Cash, A. and Driscoll, D.M. (2009) Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation. Mol. Cell, 35, 479-489.
11. Berry, M.J., Banu, L., Chen, Y.Y., Mandel, S.J., Kieffer, J.D., Harney, J.W. and Larsen, P.R. (1991) Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 30 untranslated region. Nature, 353, 273-276. (Pubitemid 21896772)
12. Copeland, P.R., Fletcher, J.E., Carlson, B.A., Hatfield, D.L. and Driscoll, D.M. (2000) A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. EMBO J., 19, 306-314. (Pubitemid 30042712)
13. Squires, J.E., Stoytchev, I., Forry, E.P. and Berry, M.J. (2007) SBP2 binding affinity is a major determinant in differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay. Mol. Cell. Biol., 27, 7848-7855. (Pubitemid 350086418)
14. Behne, D., Hilmert, H., Scheid, S., Gessner, H. and Elger, W. (1988) Evidence for specific selenium target tissues and new biologically important selenoproteins. Biochim. Biophys. Acta., 966, 12-21.
15. Hill, K.E., Lyons, P.R. and Burk, R.F. (1992) Differential regulation of rat liver selenoprotein mRNAs in selenium deficiency. Biochem. Biophys. Res. Commun., 185, 260-263.
16. Bermano, G., Nicol, F., Dyer, J.A., Sunde, R.A., Beckett, G.J., Arthur, J.R. and Hesketh, J.E. (1996) Selenoprotein gene expression during selenium-repletion of selenium-deficient rats. Biol. Trace Elem. Res., 51, 211-223.
17. Moskovitz, J. and Stadtman, E.R. (2003) Selenium-deficient diet enhances protein oxidation and affects methionine sulfoxide reductase (MsrB) protein level in certain mouse tissues. Proc. Natl Acad. Sci. USA, 100, 7486-7490. (Pubitemid 36759996)
18. Novoselov, S.V., Kim, H.Y., Hua, D., Lee, B.C., Astle, C.M., Harrison, D.E., Friguet, B., Moustafa, M.E., Carlson, B.A., Hatfield, D.L. et al. (2010) Regulation of selenoproteins and methionine sulfoxide reductases A and B1 by age, calorie restriction, and dietary selenium in mice. Antioxid. Redox. Signal, 12, 829-838.
19. Weiss Sachdev, S. and Sunde, R.A. (2001) Selenium regulation of transcript abundance and translational efficiency of glutathione peroxidase-1 and-4 in rat liver. Biochem. J., 357, 851-858. (Pubitemid 32735166)
20. Cheng, W.H., Ho, Y.S., Ross, D.A., Valentine, B.A., Combs, G.F. and Lei, X.G. (1997) Cellular glutathione peroxidase knockout mice express normal levels of selenium-dependent plasma and phospholipid hydroperoxide glutathione peroxidases in various tissues. J. Nutr., 127, 1445-1450. (Pubitemid 27323452)
21. Fomenko, D.E., Novoselov, S.V., Natarajan, S.K., Lee, B.C., Koc, A., Carlson, B.A., Lee, T.H., Kim, H.Y., Hatfield, D.L. and Gladyshev, V.N. (2009) MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form. J. Biol. Chem., 284, 5986-5993.
22. Ho, Y.S., Magnenat, J.L., Bronson, R.T., Cao, J., Gargano, M., Sugawara, M. and Funk, C.D. (1997) Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem., 272, 16644-16651. (Pubitemid 27276497)
23. Lei, X.G., Evenson, J.K., Thompson, K.M. and Sunde, R.A. (1995) Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium. J. Nutr., 125, 1438-1446.
24. Hadley, K.B. and Sunde, R.A. (2001) Selenium regulation of thioredoxin reductase activity and mRNA levels in rat liver. J. Nutr. Biochem., 12, 693-702. (Pubitemid 33026474)
25. Jeong, D.W., Kim, E.H., Kim, T.S., Chung, Y.W., Kim, H. and Kim, I.Y. (2004) Different distributions of selenoprotein W and thioredoxin during postnatal brain development and embryogenesis. Mol. Cells, 17, 156-159. (Pubitemid 39137060)
26. Jakupoglu, C., Przemeck, G.K., Schneider, M., Moreno, S.G., Mayr, N., Hatzopoulos, A.K., de Angelis, M.H., Wurst, W., Bornkamm, G.W., Brielmeier, M. et al. (2005) Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development. Mol. Cell. Biol., 25, 1980-1988. (Pubitemid 40280160)
27. Yant, L.J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J.G., Motta, L., Richardson, A. and Prolla, T.A. (2003) The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults. Free Radic. Biol. Med., 34, 496-502. (Pubitemid 36140174)
28. Walczak, R., Westhof, E., Carbon, P. and Krol, A. (1996) A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs. RNA, 2, 367-379. (Pubitemid 26371288)
29. Fagegaltier, D., Lescure, A., Walczak, R., Carbon, P. and Krol, A. (2000) Structural analysis of new local features in SECIS RNA hairpins. Nucleic Acids Res., 28, 2679-2689. (Pubitemid 30488011)
30. Grundner-Culemann, E., Martin, G.W. 3rd, Harney, J.W. and Berry, M.J. (1999) Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes. RNA, 5, 625-635. (Pubitemid 29218453)
31. Miniard, A.C., Middleton, L.M., Budiman, M.E., Gerber, C.A. and Driscoll, D.M. (2010) Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression. Nucleic Acids Res., 38, 4807-4820.
32. Fletcher, J.E., Copeland, P.R., Driscoll, D.M. and Krol, A. (2001) The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2. RNA, 7, 1442-1453. (Pubitemid 32973230)
33. Mehta, A., Rebsch, C.M., Kinzy, S.A., Fletcher, J.E. and Copeland, P.R. (2004) Efficiency of mammalian selenocysteine incorporation. J. Biol. Chem., 279, 37852-37859. (Pubitemid 39195500)
34. Walczak, R., Carbon, P. and Krol, A. (1998) An essential non-Watson-Crick base pair motif in 30UTR to mediate selenoprotein translation. RNA, 4, 74-84. (Pubitemid 28060286)
35. Martin, G.W. 3rd, Harney, J.W. and Berry, M.J. (1998) Functionality of mutations at conserved nucleotides in eukaryotic SECIS elements is determined by the identity of a single nonconserved nucleotide. RNA, 4, 65-73. (Pubitemid 28060285)
36. Schneider, M.J., Fiering, S.N., Thai, B., Wu, S.Y., St Germain, E., Parlow, A.F., St Germain, D.L. and Galton, V.A. (2006) Targeted disruption of the type 1 selenodeiodinase gene (Dio1) results in marked changes in thyroid hormone economy in mice. Endocrinology, 147, 580-589. (Pubitemid 43008392)
37. Allamand, V., Richard, P., Lescure, A., Ledeuil, C., Desjardin, D., Petit, N., Gartioux, C., Ferreiro, A., Krol, A., Pellegrini, N. et al. (2006) A single homozygous point mutation in a 30untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy. EMBO Rep., 7, 450-454.
38. Moghadaszadeh, B., Petit, N., Jaillard, C., Brockington, M., Roy, S.Q., Merlini, L., Romero, N., Estournet, B., Desguerre, I., Chaigne, D. et al. (2001) Mutations in SEPN1 cause congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Nat. Genet., 29, 17-18. (Pubitemid 32801799)
39. Dikiy, A., Novoselov, S.V., Fomenko, D.E., Sengupta, A., Carlson, B.A., Cerny, R.L., Ginalski, K., Grishin, N.V., Hatfield, D.L. and Gladyshev, V.N. (2007) SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry, 46, 6871-6882. (Pubitemid 46906416)
40. Barnes, K.M., Evenson, J.K., Raines, A.M. and Sunde, R.A. (2009) Transcript analysis of the selenoproteome indicates that dietary selenium requirements of rats based on seleniumregulated selenoprotein mRNA levels are uniformly less than those based on glutathione peroxidase activity. J. Nutr., 139, 199-206.
41. Kryukov, G.V., Castellano, S., Novoselov, S.V., Lobanov, A.V., Zehtab, O., Guigo, R. and Gladyshev, V.N. (2003) Characterization of mammalian selenoproteomes. Science, 300, 1439-1443. (Pubitemid 36638165)
42. Oguro, A., Ohtsu, T., Svitkin, Y.V., Sonenberg, N. and Nakamura, Y. (2003) RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis. RNA, 9, 394-407. (Pubitemid 36356727)
43. Del Campo, M. and Lambowitz, A.M. (2009) Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol. Cell, 35, 598-609.
44. Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S. and Yokoyama, S. (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell, 125, 287-300.
45. Sauliere, J., Haque, N., Harms, S., Barbosa, I., Blanchette, M. and Le Hir, H. (2010) The exon junction complex differentially marks spliced junctions. Nat. Struct. Mol. Biol., 17, 1269-1271.