Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers

Science

Volumn 304, Issue 5678, 2004, Pages 1793-1797

  Shorter, James ^a   Lindquist, Susan ^a  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION (PROCESS); MATHEMATICAL MODELS; NUCLEATION; OLIGOMERS; POLYPEPTIDES; REACTION KINETICS; YEAST;

INHERITANCE PATTERNS; SELF-PERPETUATING; TRANSLATION TERMINATION;

PROTEINS;

AMYLOID; HEAT SHOCK PROTEIN 104; POLYPEPTIDE; PRION PROTEIN; PROTEIN SUP35; UNCLASSIFIED DRUG;

BIOLOGY;

ARTICLE; CATALYSIS; CONCENTRATION (PARAMETERS); FIBER; IN VITRO STUDY; INHERITANCE; MODEL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; RNA TRANSLATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMYLOID; AMYLOID BETA-PROTEIN; ANTIBODIES; BIOPOLYMERS; CATALYSIS; HEAT-SHOCK PROTEINS; HYDROLYSIS; MUTATION; PEPTIDE FRAGMENTS; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 2942722444     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1098007     Document Type: Article

References (30)

1. T. R. Serio, S. L. Lindquist, Adv. Protein Chem. 59, 391 (2001).
2. S. M. Uptain, S. Lindquist, Annu. Rev. Microbiol. 56, 703 (2002).
3. S. V. Paushkin, V. V. Kushnirov, V. N. Smirnov, M. D. Ter-Avanesyan, EMBO J. 15, 3127 (1996).
4. M. M. Patino, J. J. Liu, J. R. Glover, S. Lindquist, Science 273, 622 (1996).
5. J. J. Liu, N. Sondheimer, S. L. Lindquist, Proc. Natl. Acad. Sci. U.S.A. 99 (suppl. 4), 16446 (2002).
6. D. S. Kryndushkin, I. M. Alexandrov, M. D. Ter-Avanesyan, V. V. Kushnirov, J. Biol. Chem. 278, 49636 (2003).
7. Y. Kimura, S. Koitabashi, T. Fujita, Cell Struct. Funct. 28, 187 (2003).
8. J. R. Glover et al., Cell 89, 811 (1997).
9. A. H. DePace, J. S. Weissman, Nature Struct. Biol. 9, 389 (2002).
10. T. R. Serio et al., Science 289, 1317 (2000).
11. T. Scheibel, S. L. Lindquist Nature Struct. Biol. 8, 958 (2001).
12. T. Scheibel, J. Bloom, S. L. Lindquist, Proc. Natl. Acad. Sci. U.S.A. 101, 2287 (2004).
13. M. Tanaka, P. Chien, N. Naber, R. Cooke, J. S. Weissman, Nature 428, 323 (2004).
14. Y. O. Chernoff, S. L. Lindquist, B. Ono, S. G. Inge-Vechtomov, S. W. Liebman, Science 268, 880 (1995).
15. R. D. Wegrzyn, K. Bapat, G. P. Newnam, A. D. Zink, Y. O. Chernoff, Mol. Cell. Biol. 21, 4656 (2001).
16. J. R. Glover, S. Lindquist, Cell 94, 73 (1998).
17. Very similar results were obtained when fibrillization was monitored by sodium dodecyl sulfate-resistance, sedimentation, EM, thioflavin T (ThT) fluorescence, 8-anilino-naphthalene-sulfonic acid (ANS) fluorescence, protease resistance, and turbidity.
18. E. C. Schirmer, S. Lindquist, Proc. Natl. Acad. Sci. U.S.A. 94, 13932 (1997).
19. M. E. Huff, W. E. Balch, J. W. Kelly, Curr. Opin. Struct. Biol. 13, 674 (2003).
20. R. Kayed et al., Science 300, 486 (2003).
21. B. O'Nuallain, R. Wetzel, Proc. Natl. Acad. Sci. U.S.A. 99, 1485 (2002).
22. J. Shorter, S. Lindquist, unpublished data.
23. D. A. Hattendorf, S. L. Lindquist, Proc. Natl. Acad. Sci. U.S.A. 99, 2732 (2002).
24. D. A. Hattendorf, S. L. Lindquist, EMBO J. 21, 12 (2002).
25. J. Shorter, S. Lindquist, in preparation.
26. A. G. Cashikar et al., Mol. Cell 9, 751 (2002).
27. S. Narayanan, B. Bosl, S. Walter, B. Reif, Proc. Natl. Acad. Sci. U.S.A. 100, 9286 (2003).
28. S. Lee et al., Cell 115, 229 (2003).
29. K. Si, S. Lindquist, E. R. Kandel, Cell 115, 879 (2003).
30. We are indebted to A. Cashikar for expert advice and assistance, Lindquist lab members for comments on the manuscript, C. Glabe for oligomer-specific antibody, R. Wetzel for antibody to amyloid, N. Watson for EM assistance, and F. Tsai for purified ClpB from Thermus thermophilus. Supported by a Charles A. King Trust postdoctoral fellowship (J.S.) and NIH grant no. GM25874 and a DuPont MIT Alliance grant (S.L.).