Small angle X-ray scattering study of the yeast prion Ure2p

Biochemical and Biophysical Research Communications

Volumn 311, Issue 2, 2003, Pages 525-532

  Zhu, Li ^a   Kihara, Hiroshi ^b   Kojima, Masaki ^c   Zhou, Jun Mei ^a   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b KANSAI MEDICAL UNIVERSITY   (Japan)

^c TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

Aggregation; Amyloid; Association; Cross linking; Dimer; Dissociation; Protein folding; Residual structure; Small angle X ray scattering; Ure2

Indexed keywords

3,3' DITHIOBIS(SUCCINIMIDYL PROPIONATE); PROTEIN; PROTEIN URE2; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; DENATURATION; NONHUMAN; PRION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; YEAST;

EID: 0242268096     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.10.027     Document Type: Article

References (37)

1. Taylor K.L., Cheng N., Williams R.W., Steven A.C., Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science. 283:1999;1339-1342.
2. Perrett S., Freeman S.J., Butler P.J.G., Fersht A.R. Equilibrium folding properties of the yeast prion protein determinant Ure2. J. Mol. Biol. 290:1999;331-345.
3. Lacroute F. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106:1971;519-522.
4. Coshigano P.W., Magasanik B. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione S-transferases. Mol. Cell. Biol. 11:1991;822-832.
5. Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 264:1994;566-569.
6. Masison D.C., Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science. 270:1995;93-95.
7. Thual C., Komar A.A., Bousset L., Fernandez-Bellot E., Cullin C., Melki R. Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J. Biol. Chem. 274:1999;13666-13674.
8. Bousset L., Belrhali H., Janin J., Melki R., Morera S. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure. 9:2001;39-46.
9. Umlaud T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl. Acad. Sci. USA. 98:2001;1459-1464.
10. Zhou J.M., Zhu L., Balny C., Perrett S. Pressure denaturation of the yeast prion protein Ure2. Biochem. Biophys. Res. Commun. 287:2001;147-152.
11. Thual C., Bousset L., Komar A., Walter S., Buchner J., Cullin C., Melki R. Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry. 40:2001;1764-1773.
12. Galani D., Fersht A.R., Perrett S. Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates. J. Mol. Biol. 315:2002;213-227.
13. Zhu L., Zhang X.J., Wang L.Y., Zhou J.M., Perrett S. Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. J. Mol. Biol. 328:2003;235-254.
14. Glatter O., Kratky O. Small Angle X-ray Scattering. 1982;Academic Press, London.
15. Lattman E.E. Small angle scattering studies of protein folding. Curr. Opin. Struct. Biol. 4:1994;87-92.
16. Kataoka M., Goto Y. X-ray solution scattering studies of protein folding. Fold. Des. 1:1996;R107-R114.
17. Doniach S. Changes in biomolecular conformation seen by small angle X-ray scattering. Chem. Rev. 101:2001;1763-1778.
18. Semisotnov G.V., Kihara H., Kotova N.V., Kimura K., Amemiya Y., Wakabayashi K., Serdyuk I.N., Timchenko A.A., Chiba K., Nikaido K., Ikura T., Kuwajima K. Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J. Mol. Biol. 262:1996;559-574.
19. Jaenicke R., Rudolph R. Refolding and association of oligomeric proteins. Methods Enzymol. 131:1986;218-250.
20. 35S]dithiobis(succinimidyl propionate). J. Mol. Biol. 104:1976;243-261.
21. Zhu L., Fan Y.X., Zhou J.M. The influence of intersubunit cross-linking on the conformational changes of creatine kinase during denaturation by guanidine hydrochloride. Biochem. Mol. Biol. Inter. 43:1997;207-216.
22. He B., Zhang Y., Zhang T., Zhou H.M. Dissociation of creatine kinase under different denaturation conditions. Biochemistry (Mosc.). 63:1998;1302-1306.
23. Maddelein M.L., Wickner R.B. Two prion-inducing regions of Ure2p are nonoverlapping. Mol. Cell. Biol. 19:1999;4516-4524.
24. Amemiya Y., Wakabayashi K., Hamanaka T., Wakabayashi T., Hashizume H. Design of a small-angle X-ray diffractometer using synchrotron radiation at the photon factory. Nucl. Instr. Methods. 208:1983;471-477.
25. K. Ito, PhD Thesis, University of Tokyo (1999).
26. Ito K., Kamikubo H., Arai M., Kuwajima K., Amemiya Y., Endo T. Calibration method for contrast reduction problem in the X-ray image-intensifier. Photon Factory Acitivity Rep. 18:2000;275.
27. Garcia P., Serrano L., Durand D., Rico M., Bruix M. NMR and SAXS characterization of the denatured state of the chemotactic protein CheY; implications for protein folding initiation. Protein Sci. 10:2001;1100-1112.
28. Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249:1995;215-228.
29. Kataoka M., Hagihara Y., Mihara K., Goto Y. Molten globule of cytochrome. c studies by small angle X-ray scattering J. Mol. Biol. 229:1993;591-596.
30. Kamatari Y.O., Konno T., Kataoka M., Akasaka K. The methanol-induced globular and expanded denatured states of cytochrome. c: a study by CD fluorescence, NMR and small-angle X-ray scattering J. Mol. Biol. 259:1996;512-523.
31. Konno T., Kamatari Y.O., Kataoka M., Akasaka K. Urea-induced conformational changes in cold- and heat-denatured states of a protein, Streptomyces subtilisin inhibitor. Protein Sci. 6:1997;2242-2249.
32. Uversky V.N., Li J., Fink A.L. Trimethylamine-. N -oxide-induced folding α-synuclein FEBS Lett. 509:2001;31-35.
33. Chen L., Hodgson K.O., Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261:1996;658-671.
34. Segel D.J., Bachmann A., Hofrichter J., Hodgson K.O., Doniach S., Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. J. Mol. Biol. 288:1999;489-499.
35. Briggs M.M., Capaldi R.A. Near-neighbor relationships of the subunits of cytochrome. c oxidase Biochemistry. 16:1977;73-77.
36. Zhou J.M., Fan Y.X., Kihara H., Kimura K., Amemiya Y. Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation. FEBS Lett. 415:1997;183-185.
37. Fay N., Inoue Y., Bousset L., Taguchi H., Melki R. Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterization. J. Biol. Chem. 278:2003;30199-30205.