The cryo-EM structure of a ribosome-Ski2-Ski3-Ski8 helicase complex

Science

Volumn 354, Issue 6318, 2016, Pages 1431-1433

  Schmidt, Christian ^a   Kowalinski, Eva ^b   Shanmuganathan, Vivekanandan ^a   Defenouillère, Quentin ^c,d   Braunger, Katharina ^a   Heuer, André ^a   Pech, Markus ^a   Namane, Abdelkader ^c   Berninghausen, Otto ^a   Fromont Racine, Micheline ^c   Jacquier, Alain ^c   Conti, Elena ^b   Becker, Thomas ^a   Beckmann, Roland ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c CNRS   (France)

^d SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; MESSENGER RNA; RIBOSOME RNA; RIBOSOME SKI2 SKI3 SKI8 HELICASE COMPLEX; UNCLASSIFIED DRUG; DNA HELICASE; EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; FUNGAL RNA; NUCLEAR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SKI2 PROTEIN, S CEREVISIAE; SKI3 PROTEIN, S CEREVISIAE; SKI8 PROTEIN, S CEREVISIAE;

BIOCHEMISTRY; CELL ORGANELLE; ELECTROMAGNETIC METHOD; ELECTRON MICROSCOPY; MOLECULAR ANALYSIS; RNA;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; ELECTRON TOMOGRAPHY; EXOSOME; NONHUMAN; PRIORITY JOURNAL; RIBOSOME; RNA DEGRADATION; RNA STRUCTURE; SMALL RIBOSOMAL SUBUNIT; TURNOVER TIME; CRYOELECTRON MICROSCOPY; ENZYMOLOGY; LARGE RIBOSOMAL SUBUNIT; METABOLISM; PROTEIN CONFORMATION; RNA STABILITY; SACCHAROMYCES CEREVISIAE; ULTRASTRUCTURE;

CRYOELECTRON MICROSCOPY; DNA HELICASES; EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; NUCLEAR PROTEINS; PROTEIN CONFORMATION; RIBOSOME SUBUNITS, LARGE, EUKARYOTIC; RNA STABILITY; RNA, FUNGAL; RNA, MESSENGER; RNA, RIBOSOMAL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 85006265895     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf7520     Document Type: Article

References (25)

1. B. Roy, A. Jacobson, Trends Genet. 29, 691-699 (2013).
2. C. J. Shoemaker, R. Green, Nat. Struct. Mol. Biol. 19, 594-601 (2012).
3. M. K. Doma, R. Parker, Nature 440, 561-564 (2006).
4. R. Parker, Genetics 191, 671-702 (2012).
5. W. Hu, T. J. Sweet, S. Chamnongpol, K. E. Baker, J. Coller, Nature 461, 225-229 (2009).
6. W. Hu, C. Petzold, J. Coller, K. E. Baker, Nat. Struct. Mol. Biol. 17, 244-247 (2010).
7. V. Pelechano, W. Wei, L. M. Steinmetz, Cell 161, 1400-1412 (2015).
8. S. Antic, M. T. Wolfinger, A. Skucha, S. Hosiner, S. Dorner, Mol. Cell. Biol. 35, 2309-2320 (2015).
9. F. Halbach, P. Reichelt, M. Rode, E. Conti, Cell 154, 814-826 (2013).
10. Y. Araki et al., EMBO J. 20, 4684-4693 (2001).
11. A. van Hoof, P. A. Frischmeyer, H. C. Dietz, R. Parker, Science 295, 2262-2264 (2002).
12. P. A. Frischmeyer et al., Science 295, 2258-2261 (2002).
13. G. C. Atkinson, S. L. Baldauf, V. Hauryliuk, BMC Evol. Biol. 8, 290 (2008).
14. E. Kowalinski, A. Schuller, R. Green, E. Conti, Structure 23, 1336-1343 (2015).
15. E. Kowalinski et al., Mol. Cell 63, 125-134 (2016).
16. Q. Defenouillère et al., Proc. Natl. Acad. Sci. U.S.A. 110, 5046-5051 (2013).
17. F. Halbach, M. Rode, E. Conti, RNA 18, 124-134 (2012).
18. A. Ben-Shem et al., Science 334, 1524-1529 (2011).
19. C. Schmidt et al., Nucleic Acids Res. 44, 1944-1951 (2016).
20. M. Thoms et al., Cell 162, 1029-1038 (2015).
21. J. R. Weir, F. Bonneau, J. Hentschel, E. Conti, Proc. Natl. Acad. Sci. U.S.A. 107, 12139-12144 (2010).
22. N. T. Ingolia, S. Ghaemmaghami, J. R. S. Newman, J. S. Weissman, Science 324, 218-223 (2009).
23. V. Presnyak et al., Cell 160, 1111-1124 (2015).
24. S. Ghaemmaghami et al., Nature 425, 737-741 (2003).
25. X. Qu et al., Nucleic Acids Res. 26, 4068-4077 (1998).