Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1

Science

Volumn 331, Issue 6018, 2011, Pages 730-736

  Rabl, Julius ^a   Leibundgut, Marc ^a   Ataide, Sandro F ^a   Haag, Andrea ^a   Ban, Nenad ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; INITIATION FACTOR 1; RECEPTOR FOR ACTIVATED C KINASE 1; RIBOSOME PROTEIN; RNA 18S; RPS4E PROTEIN; RPS6E PROTEIN; UNCLASSIFIED DRUG;

BACTERIUM; CILIATE; CRYSTAL STRUCTURE; EUKARYOTE; PROTEIN;

40S RIBOSOME SUBUNIT; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; RIBOSOME SUBUNIT; RNA STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TETRAHYMENA THERMOPHILA; TRANSLATION INITIATION;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; EUKARYOTIC INITIATION FACTOR-1; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTOZOAN PROTEINS; RIBOSOMAL PROTEINS; RIBOSOME SUBUNITS, SMALL, EUKARYOTIC; RNA, MESSENGER; RNA, PROTOZOAN; RNA, RIBOSOMAL, 18S; SIGNAL TRANSDUCTION; TETRAHYMENA THERMOPHILA;

BACTERIA (MICROORGANISMS); EUKARYOTA; TETRAHYMENA THERMOPHILA;

EID: 79951510534     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1198308     Document Type: Article

References (58)

1. T. M. Schmeing, V. Ramakrishnan, Nature 461, 1234 (2009).
2. J. Dresios, P. Panopoulos, D. Synetos, Mol. Microbiol. 59, 1651 (2006).
3. D. J. Taylor et al., Structure 17, 1591 (2009).
4. B. S. Laursen, H. P. Sørensen, K. K. Mortensen, H. U. Sperling-Petersen, Microbiol. Mol. Biol. Rev. 69, 101 (2005).
5. R. J. Jackson, C. U. Hellen, T. V. Pestova, Nat. Rev. Mol. Cell Biol. 11, 113 (2010).
6. N. Sonenberg, A. G. Hinnebusch, Cell 136, 731 (2009).
7. D. Silvera, S. C. Formenti, R. J. Schneider, Nat. Rev. Cancer 10, 254 (2010).
8. I. Zemp, U. Kutay, FEBS Lett. 581, 2783 (2007).
9. P. Chandramouli et al., Structure 16, 535 (2008).
10. T. Becker et al., Science 326, 1369 (2009); 10.1126/science.1178535.
11. S. Bhushan et al., Nat. Struct. Mol. Biol. 17, 313 (2010).
12. J. P. Armache et al., Proc. Natl. Acad. Sci. U.S.A. 107, 19748 (2010).
13. J. P. Armache et al., Proc. Natl. Acad. Sci. U.S.A. 107, 19754 (2010).
14. A. Ben-Shem, L. Jenner, G. Yusupova, M. Yusupov, Science 330, 1203 (2010).
15. W. M. Clemons Jr. et al., Nature 400, 833 (1999).
16. C. M. Fletcher, T. V. Pestova, C. U. Hellen, G. Wagner, EMBO J. 18, 2631 (1999).
17. M. Reibarkh et al., J. Biol. Chem. 283, 1094 (2008).
18. I. B. Lomakin, V. G. Kolupaeva, A. Marintchev, G. Wagner, T. V. Pestova, Genes Dev. 17, 2786 (2003).
19. L. A. Passmore et al., Mol. Cell 26, 41 (2007).
20. S. M. Coyle, W. V. Gilbert, J. A. Doudna, Mol. Cell. Biol. 29, 1626 (2009).
21. O. Meyuhas, Int. Rev. Cell Mol. Biol. 268, 1 (2008).
22. See supporting material on Science Online.
23. J. J. Cannone et al., BMC Bioinformatics 3, 2 (2002).
24. G. Alkemar, O. Nygård, Biochemistry 45, 8067 (2006).
25. K. Ye et al., Proc. Natl. Acad. Sci. U.S.A. 106, 13808 (2009).
26. K. L. Redman, M. Rechsteiner, Nature 338, 438 (1989).
27. T. Lacombe et al., Mol. Microbiol. 72, 69 (2009).
28. S. Takyar, R. P. Hickerson, H. F. Noller, Cell 120, 49 (2005).
29. M. A. Borovinskaya, S. Shoji, J. M. Holton, K. Fredrick, J. H. Cate, ACS Chem. Biol. 2, 545 (2007).
30. T. Kaminishi et al., Structure 15, 289 (2007).
31. A. Korostelev et al., Proc. Natl. Acad. Sci. U.S.A. 104, 16840 (2007).
32. A. V. Komarova, L. S. Tchufistova, E. V. Supina, I. V. Boni, RNA 8, 1137 (2002).
33. J. Sengupta, R. K. Agrawal, J. Frank, Proc. Natl. Acad. Sci. U.S.A. 98, 11991 (2001).
34. M. A. Sørensen, J. Fricke, S. Pedersen, J. Mol. Biol. 280, 561 (1998).
35. B. T. Wimberly et al., Nature 407, 327 (2000).
36. L. D. Kapp, J. R. Lorsch, Annu. Rev. Biochem. 73, 657 (2004).
37. M. Bycroft, T. J. P. Hubbard, M. Proctor, S. M. V. Freund, A. G. Murzin, Cell 88, 235 (1997).
38. L. Palm et al., J. Biol. Chem. 270, 6000 (1995).
39. J. Nilsson, J. Sengupta, J. Frank, P. Nissen, EMBO Rep. 5, 1137 (2004).
40. T. Sunami et al., J. Biol. Chem. 285, 4587 (2010).
41. K. Pachler et al., FEMS Yeast Res. 5, 271 (2004).
42. N. Sang et al., J. Biol. Chem. 276, 27026 (2001).
43. A. Gallina, F. Rossi, G. Milanesi, Virology 283, 7 (2001).
44. P. R. Smith et al., J. Virol. 74, 3082 (2000).
45. J. Reinhardt, T. Wolff, Vet. Microbiol. 74, 87 (2000).
46. A. J. Link et al., Nat. Biotechnol. 17, 676 (1999).
47. S. Baum, M. Bittins, S. Frey, M. Seedorf, Biochem. J. 380, 823 (2004).
48. P. A. Kiely et al., J. Biol. Chem. 284, 20263 (2009).
49. D. Maag, J. R. Lorsch, J. Mol. Biol. 330, 917 (2003).
50. J. S. Nanda et al., J. Mol. Biol. 394, 268 (2009).
51. Y. Yu et al., Nucleic Acids Res. 37, 5167 (2009).
52. A. P. Carter et al., Science 291, 498 (2001); 10.1126/science.1057766.
53. M. Selmer et al., Science 313, 1935 (2006); 10.1126/science.1131127.
54. B. Castilho-Valavicius, H. Yoon, T. F. Donahue, Genetics 124, 483 (1990).
55. H. J. Yoon, T. F. Donahue, Mol. Cell. Biol. 12, 248 (1992).
56. Y. N. Cheung et al., Genes Dev. 21, 1217 (2007).
57. A. Dallas, H. F. Noller, Mol. Cell 8, 855 (2001).
58. All data were collected at the Swiss Light Source (SLS, Paul Scherrer Institut, Villigen). We thank C. Schulze-Briese, A. Pauluhn, R. Bingel-Erlenmeyer, M. Müller, and T. Tomizaki for their outstanding support at the SLS; B. Blattmann from the NCCR crystallization facility for screening; R. Brunisholz for help with mass spectroscopy; N. Katheder, D. Baretic, and M. Weisser for their work during the initial phase of the project; S. Arpagaus for preparation of the material; T. Maier for advice during phasing; D. Böhringer for critically reading the manuscript; all members of the Ban laboratory for suggestions and discussions; and A. Brünger for providing a prerelease version of the CNS 1.3 refinement program. Supported by the Swiss National Science Foundation (SNSF), the National Center of Excellence in Research (NCCR) Structural Biology program of the SNSF, and European Research Council grant 250071 under the European Community's Seventh Framework Programme (N.B.), and the Max Roessler prize to N.B. Coordinates and structure factors have been deposited in the Protein Data Bank (PDB) with accession codes 2xzm and 2xzn. ETH Zürich has filed a patent application to use the crystals and the coordinates of the 40S ribosomal subunit for developing compounds that can interfere with eukaryotic translation.