Translational tuning optimizes nascent protein folding in cells

Science

Volumn 348, Issue 6233, 2015, Pages 444-448

  Kim, Soo Jung ^a   Yoon, Jae Seok ^a   Shishido, Hideki ^a   Yang, Zhongying ^a   Rooney, LeeAnn A ^a   Barral, Jose M ^b   Skach, William R ^a,c  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b University of Texas Medical Branch School of Medicine   (United States)

^c CYSTIC FIBROSIS FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; ASPARTIC ACID; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; CODON;

GENE EXPRESSION; PROTEIN; REACTION KINETICS;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CELLS; CODON USAGE; CRYSTAL STRUCTURE; FLUORESCENCE RESONANCE ENERGY TRANSFER; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN SYNTHESIS; RADIOIMMUNOPRECIPITATION; RIBOSOME; SURFACE PROPERTY; BIOSYNTHESIS; CHEMISTRY; CODON; GENETICS; HUMAN; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RNA TRANSLATION;

AMINO ACID SEQUENCE; CODON; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; PEPTIDE CHAIN ELONGATION, TRANSLATIONAL; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES;

EID: 84928385447     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaa3974     Document Type: Article

References (32)

1. E. Braselmann, J. L. Chaney, P. L. Clark, Trends Biochem. Sci. 38, 337-344 (2013).
2. K. S. Hingorani, L. M. Gierasch, Curr. Opin. Struct. Biol. 24, 81-90 (2014).
3. C. Eichmann, S. Preissler, R. Riek, E. Deuerling, Proc. Natl. Acad. Sci. U.S.A. 107, 9111-9116 (2010).
4. C. M. Kaiser, D. H. Goldman, J. D. Chodera, I. Tinoco Jr., C. Bustamante, Science 334, 1723-1727 (2011).
5. K. G. Ugrinov, P. L. Clark, Biophys. J. 98, 1312-1320 (2010).
6. E. P. O'Brien, J. Christodoulou, M. Vendruscolo, C. M. Dobson, J. Am. Chem. Soc. 133, 513-526 (2011).
7. A. Kosolapov, C. Deutsch, Nat. Struct. Mol. Biol. 16, 405-411 (2009).
8. C. Kimchi-Sarfaty et al., Science 315, 525-528 (2007).
9. G. Zhang, M. Hubalewska, Z. Ignatova, Nat. Struct. Mol. Biol. 16, 274-280 (2009).
10. P. S. Spencer, E. Siller, J. F. Anderson, J. M. Barral, J. Mol. Biol. 422, 328-335 (2012).
11. S. B. Zimmerman, A. P. Minton, Annu. Rev. Biophys. Biomol. Struct. 22, 27-65 (1993).
12. S. R. McGuffee, A. H. Elcock, PLOS Comput. Biol. 6, e1000694 (2010).
13. F. Willmund et al., Cell 152, 196-209 (2013).
14. A. Mashaghi et al., Nature 500, 98-101 (2013).
15. I. M. Sander, J. L. Chaney, P. L. Clark, J. Am. Chem. Soc. 136, 858-861 (2014).
16. M. Zhou et al., Nature 495, 111-115 (2013).
17. L. D. Cabrita, S. T. Hsu, H. Launay, C. M. Dobson, J. Christodoulou, Proc. Natl. Acad. Sci. U.S.A. 106, 22239-22244 (2009).
18. C. A. Woolhead, P. J. McCormick, A. E. Johnson, Cell 116, 725-736 (2004).
19. A. Khushoo, Z. Yang, A. E. Johnson, W. R. Skach, Mol. Cell 41, 682-692 (2011).
20. P. K. Devaraneni et al., Cell 146, 134-147 (2011).
21. S. H. Cheng et al., Cell 63, 827-834 (1990).
22. B.-H. Qu, E. H. Strickland, P. J. Thomas, J. Biol. Chem. 272, 15739-15744 (1997).
23. C. Wang et al., Protein Sci. 19, 1932-1947 (2010).
24. A. A. Aleksandrov et al., J. Mol. Biol. 419, 41-60 (2012).
25. J. L. Mendoza et al., Cell 148, 164-174 (2012).
26. H. A. Lewis et al., J. Mol. Biol. 396, 406-430 (2010).
27. D. A. Kelkar, A. Khushoo, Z. Yang, W. R. Skach, J. Biol. Chem. 287, 2568-2578 (2012).
28. J. L. Teem et al., Cell 73, 335-346 (1993).
29. J. Frydman, H. Erdjument-Bromage, P. Tempst, F. U. Hartl, Nat. Struct. Biol. 6, 697-705 (1999).
30. M. Chartier, F. Gaudreault, R. Najmanovich, Bioinformatics 28, 1438-1445 (2012).
31. S.Pechmann, J. Frydman,Nat.Struct. Mol. Biol. 20, 237-243 (2013).
32. F. Gloge, A. H. Becker, G. Kramer, B. Bukau, Curr. Opin. Struct. Biol. 24, 24-33 (2014).