Cold destabilization and temperature jump of the murine prion protein mPrP(23-231)

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 4, 2009, Pages 669-673

  Matsumoto, Tomoharu ^a   Nakagawa, Tatsuo ^b   Kuwata, Kazuo ^a,c  

^a GIFU UNIVERSITY   (Japan)

^b Japan Science and Technology Agency   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Cold denaturation; Folding intermediate; Laser induced temperature jump; Prion protein; Structural stability

Indexed keywords

PRION PROTEIN; UREA;

ARTICLE; CONTROLLED STUDY; DENATURATION; GENE MUTATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE MEASUREMENT;

ANIMALS; CIRCULAR DICHROISM; COLD TEMPERATURE; MICE; MICROSCOPY, FLUORESCENCE; PEPTIDE FRAGMENTS; PRIONS; PROTEIN FOLDING; PROTEIN STABILITY; RECOMBINANT PROTEINS; UREA;

MURINAE;

EID: 61649089218     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.01.005     Document Type: Article

References (27)

1. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
2. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13363-13383
3. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24 (2001) 519-550
4. Aguzzi A., and Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 116 (2004) 313-327
5. Stahl N., Baldwin M.A., Teplow D.B., Hood L., Gibson B.W., Burlingame A.L., and Prusiner S.B. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32 (1993) 1991-2002
6. Caughey B.W., Dong A., Bhat K.S., Ernst D., Hayes S.F., and Caughey W.S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30 (1991) 7672-7680
7. Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F.E., and Prusiner S.B. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 10962-10966
8. Kuwata K., Nishida N., Matsumoto T., Kamatari Y.O., Hosokawa-Muto J., Kodama K., Nakamura H.K., Kimura K., Kawasaki M., Takakura Y., Shirabe S., Takata J., Kataoka Y., and Katamine S. Hot spots in prion protein for pathogenic conversion. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11921-11926
9. Legname G., Baskakov I.V., Nguyen H.O., Riesner D., Cohen F.E., DeArmond S.J., and Prusiner S.B. Synthetic mammalian prions. Science 305 (2004) 673-676
10. Castilla J., Saa P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
11. Sc) into contiguous membranes. EMBO J. 21 (2002) 1031-1040
12. Bessen R.A., and Marsh R.F. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J. Virol. 66 (1992) 2096-2101
13. Sc molecules with different conformers. Nat. Med. 4 (1998) 1157-1165
14. Sc?. Biochemistry 41 (2002) 12277-12283
15. Cordeiro Y., Kraineva J., Gomes M.P., Lopes M.H., Martins V.R., Lima L.M., Foguel D., Winter R., and Silva J.L. The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys. J. 89 (2005) 2667-2676
16. Heindl P., Garcia A.F., Butz P., Pfaff E., and Tauscher B. Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions. Biochim. Biophys. Acta 1764 (2006) 552-557
17. Martins S.M., Chapeaurouge A., and Ferreira S.T. Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature. J. Biol. Chem. 278 (2003) 50449-50455
18. Torrent J., Alvarez-Martinez M.T., Liautard J.P., and Lange R. Modulation of prion protein structure by pressure and temperature. Biochim. Biophys. Acta 1764 (2006) 546-551
19. Apetri A.C., and Surewicz W.K. Kinetic intermediate in the folding of human prion protein. J. Biol. Chem. 277 (2002) 44589-44592
20. Apetri A.C., Maki K., Roder H., and Surewicz W.K. Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J. Am. Chem. Soc. 128 (2006) 11673-11678
21. Ballew R.M., Sabelko J., and Gruebele M. Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 5759-5764
22. Kamatari Y.O., Nakamura H.K., and Kuwata K. Strange kinetic phase in the extremely early folding process of beta-lactoglobulin. FEBS Lett. 581 (2007) 4463-4467
23. Wildegger G., Liemann S., and Glockshuber R. Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat. Struct. Biol. 6 (1999) 550-553
24. Hornemann S., and Glockshuber R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6010-6014
25. Hagen S.J., Hofrichter J., Szabo A., and Eaton W.A. Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 11615-11617
26. Bryngelson J.D., Onuchic J.N., Socci N.D., and Wolynes P.G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21 (1995) 167-195
27. Santoro M.M., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068