Chaperonin-encapsulation of proteins for NMR

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 4, 2010, Pages 866-871

  Tanaka, Shinji ^a   Kawata, Yasushi ^b   Otting, Gottfried ^c   Dixon, Nicholas E ^c,d   Matsuzaki, Katsumi ^a   Hoshino, Masaru ^a  

^a KYOTO UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

^c AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

^d UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

Aggregation; GroE; Molecular chaperone; NMR; Protein encapsulation

Indexed keywords

BINDING PROTEIN; CHAPERONIN;

AMINO ACID SEQUENCE; ARTICLE; ENCAPSULATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN ISOLATION; PROTEIN TARGETING;

CHAPERONIN 10; CHAPERONIN 60; CHAPERONINS; ESCHERICHIA COLI PROTEINS; HUMANS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEINS; UBIQUITIN;

EID: 76849111130     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.12.016     Document Type: Article

References (26)

1. 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. U. S. A. 94 (1997) 12366-12371
2. Salzmann M., Pervushin K., Wider G., Senn H., and Wührich K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13585-13590
3. Korzhnev D.M., Kloiber K., Kanelis V., Tugarinov V., and 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 (2004) 3964-3973
4. Lazar K.L., Kurutz J.W., Tycko R., and Meredith S.C. Encapsulation and NMR on an aggregating peptide before fibrillogenesis. J. Am. Chem. Soc. 128 (2006) 16460-16461
5. Wand A.J., Ehrhardt M.R., and Flynn P.F. High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15299-15302
6. Peterson R.W., Lefebvre B.G., and Wand A.J. High-resolution NMR studies of encapsulated proteins in liquid ethane. J. Am. Chem. Soc. 127 (2005) 10176-10177
7. Weissman J.S., Hohl C.M., Kovalenko O., Kashi Y., Chen S., Braig K., Saibil H.R., Fenton W.A., and Horwich A.L. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83 (1995) 577-587
8. Inobe T., Makio T., Takasu-Ishikawa E., Terada T.P., and Kuwajima K. Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP. Biochim. Biophys. Acta 1545 (2001) 160-173
9. Mizobata T., Akiyama Y., Ito K., Yumoto N., and Kawata Y. Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. J. Biol. Chem. 267 (1992) 17773-17779
10. Kawata Y., Kawagoe M., Hongo K., Miyazaki T., Higurashi T., Mizobata T., and Nagai J. Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry 38 (1999) 15731-15740
11. Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
12. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
13. Braig K., Otwinowskl Z., Hegde R., Boisvert D.C., Joachimiak A., Horwich A.L., and Sigler P.B. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371 (1994) 578-586
14. 7 chaperonin complex. Nature 388 (1997) 741-750
15. Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., and Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84 (1996) 481-490
16. Mayhew M., de Silva A.C.R., Martin J., Erdjument-Bromage H., Tempst P., and Hartl F.U. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379 (1996) 420-426
17. Rye H.S., Burston S.G., Fenton W.A., Beechem J.M., Xu Z., Sigler P.B., and Horwich A.L. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388 (1997) 792-798
18. Rye H.S., Roseman A.M., Chen S., Furtak K., Fenton W.A., Saibil H.R., and Horwich A.L. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97 (1999) 325-328
19. Chen L., and Sigler P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell 99 (1999) 757-768
20. Wang J., and Chen L. Domain motions in GroEL upon binding of an oligopeptide. J. Mol. Biol. 334 (2003) 489-499
21. Horst R., Bertelsen E.B., Fiaux J., Wider G., Horwich A.L., and Wüthrich K. Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 12748-12753
22. Kanno R., Koike-Takeshita A., Yokoyama K., Taguchi H., and Mitsuoka K. Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity. Structure 17 (2009) 287-293
23. Vijay-Kumar S., Bugg C.E., and Cook W.J. Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194 (1987) 531-544
24. Sakikawa C., Taguchi H., Makino Y., and Yoshida M. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274 (1999) 21251-21256
25. Miyazaki T., Yoshimi T., Furutsu Y., Hongo K., Mizobata T., Kanemori M., and Kawata Y. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. J. Biol. Chem. 277 (2002) 50621-50628
26. Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55