Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles

Nature

Volumn 423, Issue 6940, 2003, Pages 628-632

  Ishii, Daisuke ^a   Kinbara, Kazushi ^a   Ishida, Yasuhiro ^a   Ishii, Noriyuki ^b   Okochi, Mina ^c   Yohda, Masafumi ^c   Aida, Takuzo ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; PHOTOLUMINESCENCE; PROTEINS; SEMICONDUCTOR MATERIALS;

CHEMICAL STABILITY;

NANOSTRUCTURED MATERIALS;

ADENOSINE TRIPHOSPHATE; CHAPERONIN; NANOPARTICLE;

NANOTECHNOLOGY; SEMICONDUCTOR INDUSTRY;

ARTICLE; BIOLOGY; CATALYSIS; ESCHERICHIA COLI; LUMINESCENCE; MICROENCAPSULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SEMICONDUCTOR; THERMOSTABILITY; THERMUS THERMOPHILUS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN 60; ELECTRON TRANSPORT; ESCHERICHIA COLI; GROEL PROTEIN; MAGNESIUM; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; NANOTECHNOLOGY; POTASSIUM; SEMICONDUCTORS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 0037497251     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01663     Document Type: Article

References (26)

1. Alivisatos, A. P. Semiconductor clusters, nanocrystals, and quantum dots. Science 271, 933-937 (1996).
2. Schmid, G. et al. Current and future applications of nanoclusters. Chem. Soc. Rev. 28, 179-185 (1999).
3. Meldrum, F. C., Heywood, B. R. & Mann, S. Magnetoferittin - in vitro synthesis of a novel magnetic protein. Science 257, 522-523 (1992).
4. Wong, K. K. W. & Mann, S. Biomimetic synthesis of cadmium sulfide-ferritin nanocomposites. Adv. Mater. 8, 928-932 (1996).
5. Shenton, W., Pum, D., Sleytr, U. B. & Mann, S. Biocrystal templating of CdS superlattices using self-assembled bacterial S-layers. Nature 389, 585-587 (1997).
6. Balogh, L. & Tomalia, D. A. Poly(amidoamine) dendrimer-templated nanocomposites. I. Synthesis of zerovalent copper nanocluslers. J. Am. Chem. Soc. 120, 7355-7356 (1998).
7. Lemon, B. I. & Crooks, R. M. Preparation and characterization ofdendrimer-encapsulated CdS semiconductor quantum dots. J. Am. Chem. Soc. 122, 12886-12887 (2000).
8. Shenton, W., Mann, S., Cölfen, H., Bacher, A. & Fischer, M. Synthesis of nanophase iron oxide in lumazine synthase capsids. Angew. Chem. Int. Edn Engl. 40, 442-445 (2001).
9. McMillan, R. A. et al. Ordered nanoparticle arrays formed on engineered chaperonin protein templates. Nature Mater. 1, 247-252 (2002).
10. Roseman, A. M., Chen, S., White, H., Braig, K. & Saibil, H. R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in groEL. Cell 87, 241-251 (1996).
11. Ranson, N. A. et al. ATP-bound states of groEL captured by cryo-electron microscopy. Cell 107, 869-879 (2001).
12. Hendrix, R. W. Purification and properties of groE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129, 375-392 (1979).
13. Braig, K. et al. The crystal structure of the bacterial chaperonin groEL at 2.8 Å. Nature 371, 578-586 (1994).
14. Taguchi, H., Konishi, J., Ishii, N. & Yoshida, M. A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzymes. J. Biol. Chem. 266, 22411-22418 (1991).
15. Amada, K. et al. Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8. J. Biochem. 118, 347-354 (1995).
16. Ishii, N., Taguchi, H., Sumi, M. & Yoshida, M. Structure ofholo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each. FEBS Lett. 299, 169-174 (1992).
17. Ishii, N., Taguchi, H., Sasabe, H. & Yoshida, M. Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody. J. Mol. Biol. 236, 691-696 (1994).
18. Murakoshi, K. et al. Preparation of size-controlled hexagonal CdS nanocrystallites and the characteristics of their surface structures. J. Chem. Soc. Faraday Trans. 94, 579-586 (1998).
19. Hosokawa, H. et al. In-situ EXAFS observation of the surface structure of colloidal CdS nanocrystallites in N,N-dimethylformamide. J. Phys. Chem. 100, 6649-6656 (1996).
20. Brus, L. E. Electron-electron and electron-hole interactions in small semiconductor crystallites: The size dependence of the lowest excited electronic state. J. Chem. Phys. 80, 4403-4409 (1984).
21. Ramsden, J. J. & Grätzel, M. Photoluminescence of small cadmium sulfide particles. J. Chem. Soc. Faraday Trans. 1 80, 919-933 (1984).
22. Henglein, A. Photochemistry of colloidal cadmium sulfide. 2. Effects of adsorbed methyl viologen and of colloidal platinum. J. Phys. Chem. 86, 2291-2293 (1982).
23. Llorca, O., Galán, A., Carrascosa, J. L., Muga, A. & Valpuesta, J. M. GroEL under heat-shock. J. Biol. Chem. 273, 32587-32594 (1998).
24. Martin, J., Horwich, A. L. & Hartl, F. U. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258, 995-998 (1992).
25. Goloubinoff, P., Christeller, J. T., Gatenby, A. A. & Lorimer, G. H. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342, 884-889 (1989).
26. Todd, M. J., Viitanen, P. V. & Lorimer, G. H. Hydrolysis of adenosine 5′-triphosphate by Escherichia coli groEL: effects of groES and potassium ion. Biochemistry 32, 8560-8567 (1993).