- 1) Prusiner, S. B., Prions. Proc. Natl. Acad. Sci. USA, 95, 13363–13383 (1998).
- 2) Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Kataoka, Y., Houtani, T., Shirabe, S., Okada, H., Hasegawa, S., Miyamoto, T., and Noda, T., Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature (London), 380, 528–531 (1996).
- 3) Wickner, R. B., [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science, 264, 566–569 (1994).
- 4) Umland, T. C., Taylor, K. L., Rhee, S., Wickner, R. B., and Davies, D. R., The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA, 98, 1459–1464 (2001).
- 5) Tuite, M. F., Psi no more for yeast prions. Nature (London), 370, 327–328 (1994).
- 6) Chernoff, Y. O., Lindquist, S. L., Ono, B., Inge-Vechtomov, S. G., and Liebman, S. W., Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science, 268, 880–884 (1995).
- 7) Glover, J. R., Kowal, A. S., Schirmer, E. C., Patino, M. M., Liu, J. J., and Lindquist, S., Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell, 89, 811–819 (1997).
- 8) Derkatch, I. L., Bradley, M. E., Hong, J. Y., and Liebman, S. W., Prions affect the appearance of other prions: the story of [PIN(+)]. Cell, 106, 171–182 (2001).
- 9) Bagriantsev, S., and Liebman, S. W., Specificity of prion assembly in vivo; [PSI +] and [PIN +] form separate structures in yeast. J. Biol. Chem., 279, 51042–51048 (2004).
- 10) Liebman, S. W., Prions; the shape of a species barrier. Nature, 410, 161–162 (2001).
- 11) Nakayashiki, T., Kurtzman, C. P., Edskes, H. K., and Wickner, R. B., Yeast prions [URE3] and [PSI+] are diseases. Proc. Natl. Acad. Sci. USA, 102, 10575–10580 (2005).
- 12) Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O., Riekel, C., Grothe, R., and Eisenberg, D., Structure of the cross-beta spine of amyloid-like fibrils. Nature (London), 435, 773–777 (2005).
- 13) Krishnan, R., and Lindquist, S. L., Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature (London), 435, 765–772 (2005).
- 14) Gokhale, K. C., Newnam, G. P., Sherman, M. Y., and Chernoff, Y. O., Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem., 280, 22809–22818 (2005).
- 15) Ono, B., Tanaka, M., Awano, I., Okamoto, F., Satoh, R., Yamagishi, N., and Ishino-Arao, Y., Two new loci that give rise to dominant omnipotent suppressors in Saccharomyces cerevisiae. Curr. Genet., 16, 323–330 (1989).
- 16) Ono, B., Chernoff, Y. O., Ishino-Arao, Y., Yamagishi, N., Shinoda, S., and Inge-Vechtomov, G., Interactions between chromosomal omnipotent suppressors and extrachromosomal effecters in Saccharomyces cerevisiae. Curr. Genet., 19, 243–248 (1991).
- 17) Kushnirov, V. V., and Ter-Avanesyan, M. D., Structure and replication of yeast prions. Cell, 94, 13–16 (1998).
- 18) Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N., and Ter-Avanesyan, M. D., Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J., 15, 3127–3134 (1996).
- 19) Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N., and Ter-Avanesyan, M. D., In vitro propagation of the prion-like state of yeast Sup35 protein. Science, 277, 381–383 (1997).
- 20) Inoue, Y., Taguchi, H., Kishimoto, A., and Yoshida, M., Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. J. Biol. Chem., 279, 52319–52323 (2005).
- 21) Studier, F. W., and Moffatt, B. A., Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned gene. J. Mol. Biol., 189, 113–130 (1986).
- 22) Sambrook, J., Fritsch, E. F., and Maniatis, T., “Molecular Clonig: a Laboratory Manual” 3rd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, pp. 1.31–1.34 (1989).
- 23) Guarente, L., Yocum, R. R., and Gifford, P., A GAL10-CYC1 hybrid yeast promoter identifies the GAL4 regulatory region as an upstream site. Proc. Natl. Acad. Sci. USA, 79, 7410–7414 (1982).
- 24) Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248–254 (1976).
- 25) Habig, W. H., Pabst, M. J., and Jakoby, W. B., Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem., 249, 7130–7139 (1974).
- 26) Klunk, W. E., Pettergrew, J. W., and Abraham, D. J., Quantitative evaluation of Congo red binding to amyloid-like proteins with a β-pleated sheet conformation. J. Histchem. Cytochem., 37, 1273–1281 (1989).
- 27) Wilkinson, D. L., and Harrison, R. G., Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology (NY), 9, 443–448 (1991).
- 28) Dagkesamanskaya, A. R., Kushnirov, V. V., Paushkin, S. V., and Ter-Avanesyyan, M. D., Glutathione S-transferase fusion with the N end of Sup35p yeast protein inhibits its prion-like properties. Russ. J. Genet., 33, 504–509 (1997).
- 29) Balbirnie, M., Grothe, R., and Eisenberg, D. S., An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA, 98, 2375–2380 (2001).
Full access
Production of a Polymer-Forming Fusion Protein in Escerichia coli Strain BL21
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.