The proteasome antechamber maintains substrates in an unfolded state

Nature

Volumn 467, Issue 7317, 2010, Pages 868-871

  Ruschak, Amy M ^a   Religa, Tomasz L ^a   Breuer, Sarah ^b   Witt, Susanne ^b   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME;

ENZYME ACTIVITY; EUKARYOTE; HYDROLYSIS; PEPTIDE; PROTEIN;

ARTICLE; CONTROLLED STUDY; DYNAMICS; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOPLASMA ACIDOPHILUM;

AMINO ACID SEQUENCE; HYDROLYSIS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; PROTEIN SUBUNITS; PROTEIN UNFOLDING; THERMODYNAMICS; THERMOPLASMA;

EUKARYOTA; THERMOPLASMA;

EID: 77957970501     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09444     Document Type: Article

References (34)

1. Förster, A. & Hill, C. P. Proteasome degradation: enter the substrate. Trends Cell Biol. 13, 550-553 (2003).
2. Coux, O., Tanaka, K. & Goldberg, A. L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847 (1996). (Pubitemid 26255262)
3. Baumeister, W., Walz, J., Zü hl, F. & Seemü ller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380 (1998).
4. Marques, A. J., Palanimurugan, R., Matias, A. C., Ramos, P. C. & Dohmen, R. J. Catalytic mechanism and assembly of the proteasome. Chem. Rev. 109, 1509-1536 (2009).
5. Löwe, J. et al. Crystal structure of the 20S proteasome from the archaeon T. Acidophilum at 3.4 A resolution. Science 268, 533-539 (1995).
6. Liu, C. W., Corboy, M. J., DeMartino, G. N.& Thomas, P. J. Endoproteolytic activity of the proteasome. Science 299, 408-411 (2003).
7. Cheng, Y. Toward an atomic model of the 26S proteasome. Curr. Opin. Struct. Biol. 19, 203-208 (2009).
8. Tugarinov, V., Hwang, P. M., Ollerenshaw, J. E. & Kay, L. E. Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J. Am. Chem. Soc. 125, 10420-10428 (2003).
9. Sharon, M. et al.20S proteasomes have the potential to keep substrates in store for continual degradation. J. Biol. Chem. 281, 9569-9575 (2006).
10. Hutschenreiter, S., Tinazli, A., Model, K.&Tampé, R.Two-substrate associationwith the 20S proteasome at single-molecule level. EMBO J. 23, 2488-2497 (2004).
11. Ellis, R. J. Protein folding: importance of the Anfinsen cage. Curr. Biol. 13, R881-R883 (2003).
12. Zhou, H. X. Protein folding in confined and crowded environments. Arch. Biochem. Biophys. 469, 76-82 (2008).
13. Ruschak, A. M. & Kay, L. E. Methyl groups as probes of supra-molecular structure, Dynamics and function. J. Biomol. NMR 46, 75-87 (2010).
14. Mayor, U. et al. The complete folding pathway of a protein from nanoseconds to microseconds. Nature 421, 863-867 (2003).
15. Neudecker, P. et al. Identification of a collapsed intermediate with non-native longrange interactions on the folding pathway of a pair of Fyn SH3 domainmutants by NMR relaxation dispersion spectroscopy. J. Mol. Biol. 363, 958-976 (2006).
16. Jager, M. et al. Understanding the mechanism of beta-sheet folding from a chemical and biological perspective. Biopolymers 90, 751-758 (2008).
17. Zwickl, P., Kleinz, J. & Baumeister, W. Critical elements in proteasome assembly. Nature Struct. Biol. 1, 765-770 (1994).
18. Sprangers, R. & Kay, L. E. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622 (2007).
19. Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S. & Sykes, B. D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5, 67-81 (1995).
20. Fitzkee, N. C.&Rose, G. D. Reassessing random-coil statistics in unfolded proteins. Proc. Natl Acad. Sci. USA 101, 12497-12502 (2004).
21. Jäger, M. et al. Structure-function-folding relationship in a WW domain. Proc. Natl Acad. Sci. USA 103, 10648-10653 (2006).
22. Kubelka, J., Hofrichter, J.& Eaton, W. A. The protein folding 'speed limit'. Curr. Opin. Struct. Biol. 14, 76-88 (2004).
23. Jäger, M., Nguyen, H., Crane, J. C., Kelly, J. W. & Gruebele, M. The folding mechanism of a beta-sheet: the WW domain. J. Mol. Biol. 311, 373-393 (2001).
24. Tugarinov, V., Sprangers, R. & Kay, L. E. Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy. J. Am. Chem. Soc. 129, 1743-1750 (2007).
25. Choy, W. Y., Shortle, D. & Kay, L. E. Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of D131D. J. Am. Chem. Soc. 125, 1748-1758 (2003).
26. Battiste, J. L. & Wagner, G. Utilization of site-directed spin labeling and highresolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39, 5355-5365 (2000).
27. Clore, G. M., Tang, C. & Iwahara, J. Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement. Curr. Opin. Struct. Biol. 17, 603-616 (2007).
28. Kisselev, A. F., Songyang, Z. & Goldberg, A. L. Why does threonine, and not serine, Function as the active site nucleophile in proteasomes? J. Biol. Chem. 275, 14831-14837 (2000).
29. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing systembased on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
30. Fersht, A. Structure and Mechanism in Protein Science (Freeman, 1999).
31. Sprangers, R., Velyvis, A. & Kay, L. E. Solution NMR of supramolecular complexes: providing new insights into function. Nature Methods 4, 697-703 (2007).
32. Stollar, E. J. et al. Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics. J. Biol. Chem. 278, 43699-43708 (2003).
33. Tugarinov, V. & Kay, L. E. Relaxation rates of degenerate 1H transitions in methyl groups of proteins as reporters of side-chain dynamics. J. Am. Chem. Soc. 128, 7299-7308 (2006).
34. Matsunaga, N.& Nagashima, A. Transport properties of liquid and gaseous D2O over a wide range of temperature and pressure. J. Phys. Chem. 6, 1133-1166 (1977).