Quantitative dynamics and binding studies of the 20S proteasome by NMR

Nature

Volumn 445, Issue 7128, 2007, Pages 618-622

  Sprangers, Remco ^a   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME;

AMINO ACID; MOLECULAR ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PROTEIN;

ARTICLE; ENZYME BINDING; ENZYME STRUCTURE; ISOTOPE LABELING; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTON TRANSPORT; QUANTITATIVE ANALYSIS;

EID: 33846928691     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05512     Document Type: Article

References (29)

1. Pickart, C. M. & Cohen, R. E. Proteasomes and their kin: proteases in the machine age. Nature Rev. Mol. Cell Biol. 5, 177-187 (2004).
2. Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380 (1998).
3. Adams, J. The proteasome: a suitable antineoplastic target. Nature Rev. Cancer 4, 349-360 (2004).
4. Löwe, J. et al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268, 533-539 (1995).
5. Glickman, M. H. et al. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94, 615-623 (1998).
6. Whitby, F. G. et al. Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408, 115-120 (2000).
7. Sharon, M. et al. 20S proteasomes have the potential to keep substrates in store for continual degradation. J. Biol. Chem. 281, 9569-9575 (2006).
8. Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471 (1997).
9. Unno, M. et al. The structure of the mammalian 20S proteasome at 2.75 Å resolution. Structure 10, 609-618 (2002).
10. Kwon, Y. D., Nagy, I., Adams, P. D., Baumeister, W. & Jap, B. K. Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly. J. Mol. Biol. 335, 233-245 (2004).
11. Groll, M. et al. A gated channel into the proteasome core particle. Nature Struct. Biol. 7, 1062-1067 (2000).
12. Mittermaier, A. & Kay, L. E. New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228 (2006).
13. Tugarinov, V., Hwang, P. M. & Kay, L. E. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu. Rev. Biochem. 73, 107-146 (2004).
14. 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J. Am. Chem. Soc. 125, 10420-10428 (2003).
15. Zwickl, P., Kleinz, J. & Baumeister, W. Critical elements in proteasome assembly. Nature Struct. Biol. 1, 765-770 (1994).
16. 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl Acad. Sci. USA 94, 12366-12371 (1997).
17. Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wüthrich, K. TROSY in tripleresonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl Acad. Sci. USA 95, 13585-13590 (1998).
18. Tugarinov, V. & Kay, L. E. Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods. J. Am. Chem. Soc. 125, 13868-13878 (2003).
19. Sprangers, R., Gribun, A., Hwang, P. M., Houry, W. A. & Kay, L. E. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proc. Natl Acad. Sci. USA 102, 16678-16683 (2005).
20. Tugarinov, V., Ollerenshaw, J. E. & Kay, L. E. Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. J. Am. Chem. Soc. 127, 8214-8225 (2005).
21. 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface. Biochemistry 44, 15970-15977 (2005).
22. Forster, A., Masters, E. I., Whitby, F. G., Robinson, H. & Hill, C. P. The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol. Cell 18, 589-599 (2005).
23. Nederlof, P. M., Wang, H. R. & Baumeister, W. Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro. Proc. Natl Acad. Sci. USA 92, 12060-12064 (1995).
24. Korzhnev, D. M., Kloiber, K., Kanelis, V., Tugarinov, V. & Kay, L. E. Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. J. Am. Chem. Soc. 126, 3964-3973 (2004).
25. Benaroudj, N., Zwickl, P., Seemuller, E., Baumeister, W. & Goldberg, A. L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11, 69-78 (2003).
26. Fiaux, J., Bertelsen, E. B., Horwich, A. L. & Wüthrich, K. NMR analysis of a 900K GroEL GroES complex. Nature 418, 207-211 (2002).
27. Liu, C. W., Corboy, M. J., DeMartino, G. N. & Thomas, P. J. Endoproteolytic activity of the proteasome. Science 299, 408-411 (2003).
28. 13C labeling. Biochemistry 28, 7510-7516 (1989).
29. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).