Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein

Protein Science

Volumn 14, Issue 9, 2005, Pages 2228-2235

  Chen, Ching Ying ^a   Rojanatavorn, Kawan ^a   Clark, A Clay ^a   Shih, Jason C H ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

BSE; Enzymatic degradation; Prion; Prion surrogate protein; PrPSc; Sup35NM; Yeast prion

Indexed keywords

CONGO RED; FUNGAL PROTEIN; KERATINASE; PRION LIKE PROTEIN; PROTEINASE K; UNCLASSIFIED DRUG;

ARTICLE; ELECTRON MICROSCOPY; ENZYMATIC DEGRADATION; ESCHERICHIA COLI; FLUORESCENCE; GEL ELECTROPHORESIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; WESTERN BLOTTING; YEAST;

AMINO ACID SEQUENCE; BLOTTING, WESTERN; CONGO RED; ENDOPEPTIDASE K; ESCHERICHIA COLI; FLUORESCENCE; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PRIONS; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE; TIME FACTORS;

BACTERIA (MICROORGANISMS); BOVINAE;

EID: 24344496026     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.041234405     Document Type: Article

References (29)

1. Baskakov, I.V., Legname, G., Baldwin, M.A., Prusiner, S.B., and Cohen, F.E. 2002. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 277: 21140-21148.
2. Burger, D. and Hartsough, G.R. 1965. Encephalopathy of mink. II. Experimental and natural transmission. J. Infect. Dis. 115: 393-399.
3. Caughey, B.W., Dong, A., Bhat, K.S., Ernst, D., Hayes, S.F., and Caughey, W.S. 1991. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30: 7672-7680.
4. Chernoff, Y.O., Uptain, S.M., and Lindquist, S.L. 2002. Analysis of prion factors in yeast. Methods Enzymol. 351: 499-538.
5. Derkatch, I.L., Bradley, M.E., Zhou, P., Chernoff, Y.O., and Liebman, S.W. 1997. Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147: 507-519.
6. Gill, S.C. and von Hippel, P.H. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182: 319-326.
7. Glover, J.R., Kowal, A.S., Schirmer, E.C., Patino, M.M., Liu, J.J., and Lindquist, S.L. 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89: 811-819.
8. King, C.Y. and Diaz-Avalos, R. 2004. Protein-only transmission of three yeast prion strains. Nature 428: 319-323.
9. King, C.Y., Tittmann, P., Gross, H., Gebert, R., Aebi, M., and Wuthrich, K. 1997. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. 94: 6618-6622.
10. Klunk, W.E., Pettegrew, J.W., and Abraham, D.J. 1989. Two simple methods for quantifying low-affinity dye-substrate binding. J. Histochem. Cytochem. 37: 1293-1297.
11. Kushnirov, V.V., Kochneva-Pervukhova, N.V., Chechenova, M.B., Frolova, N.S., and Ter-Avanesyan, M.D. 2000. Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J. 19: 324-331.
12. Langeveld, J.P.M., Wang, J.J., Van de Wiel, D.F.M., Shih, G.C., Garssen, G.J., Bossers, A., and Shih, J.C.H. 2003. Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J. Infect. Dis. 188: 1782-1789.
13. Leggett, M.M., Dukes, J., and Pirie, H.M. 1990. A spongiform encephalopathy in a cat. Vet. Rec. 127: 586-588.
14. Legname, G., Baskakov, I.V., Nguyen, H.O., Riesner, D., Cohen, F.E., DeArmond, S.J., and Prusiner, S.B. 2004. Synthetic mammalian prions. Science 305: 673-676.
15. Lin, X., Lee, C.G., Casale, E.S., and Shih, J.C.H. 1992. Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain. Appl. Environ. Microbiol. 58: 3271-3275.
16. Lin, X., Wong, S.L., Miller, E.S., and Shih, J.C. 1997. Expression of the Bacillus licheniformis PWD-1 keratinase gene in B. subtilis. J. Ind. Microbiol. Biotechnol. 19: 134-138.
17. Liu, J.J., Sondheimer, N., and Lindquist, S.L. 2002. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc. Natl. Acad. Sci. 99: 16446-16453.
18. Masison, D.C. and Wickner, R.B. 1995. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270: 93-95.
19. McLeod, A.H., Murdoch, H., Dickinson, J., Dennis, M.J., Hall, G.A., Buswell, C.M., Carr, J., Taylor, D.M., Sutton, J.M., and Raven, N.D. 2004. Proteolytic inactivation of the bovine spongiform encephalopathy agent. Biochem. Biophys. Res. Commun. 317: 1165-1170.
20. Osherovich, L.Z., Cox, B.S., Tuite, M.F., and Weissman, J.S. 2004. Dissection and design of yeast prions. PLoS Biol. 2: 442-451.
21. Pan, K.M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R.J., Cohen, F.E., et al. 1993. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. 90: 10962-10966.
22. Parchi, P. and Gambetti, P. 1995. Human prion diseases. Curr. Opin. Neurol. 8: 286-293.
23. Paushkin, S.V., Kushnirov, V.V., Smirnov, V.N., and Ter-Avanesyan, M.D. 1996. 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.
24. Prusiner, S.B., Scott, M.R., DeArmond, S.J., and Cohen, F.E. 1998. Prion protein biology. Cell 93: 337-348.
25. Saupe, S.J. 2003. New anti-prion drugs make yeast blush. Trends. Biotechnol. 21: 516-519.
26. Serio, T.R., Cashikar, A.G., Moslehi, J.J., Kowal, A.S., and Lindquist, S.L. 1999. Yeast prion and its determinant, Sup35p. Methods Enzymol. 309: 649-673.
27. Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J.S. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328.
28. 6. Enz. Microb. Technol. 36: 758-765.
29. Williams, E.S. and Young, S. 1980. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis. 16: 89-98.