The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride

Biophysical Chemistry

Volumn 85, Issue 2-3, 2000, Pages 179-186

  Guo, Yuan ^a   Kammerer, Richard A ^a   Engel, Jürgen ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Helical coiled coil; Circular dichroism spectroscopy, thermodynamics; Cold and heat denaturation; Guanidinium chloride

Indexed keywords

MATRIX PROTEIN;

ARTICLE; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; TEMPERATURE; THERMODYNAMICS;

EID: 0033935599     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00119-8     Document Type: Article

References (32)

1. Bikle D.D., Munson S., Morrison N., Eisman J. Zipper protein, a newly described tropomyosin-like protein of the intestinal brush border. J. Biol. Chem. 268:1993;620-626.
2. Brands J.F. The thermaldynamics of protein denaturation. I. The denaturation of chymotrypsinogen. J. Am. Chem. Soc. 86:1964;4291-4301.
3. J.F. Brands, Comformational transition of proteins in water and in aqueous mixtures, in: S.N. Timasheff, G.D. Fasman, (Eds), Structure and Stability of Biological Macromolecules, Marcel Dekker, New York, 1969, pp. 213-290.
4. Cedervall T., Johansson M.U., Akerstrom B. Coiled-coil structure of group A streptococcal M proteins. Different temperature stability of class A and C proteins by hydrophobic-nonhydrophobic amino acid substitutions at heptad positions a and d. Biochemistry. 36:1997;4987-4994.
5. Cohen C. Why fibrous proteins are romantic. J. Struct. Biol. 122:1998;3-16.
6. Cohen C., Parry D.A. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins. 7:1990;1-15.
7. Efimov V.P., Lustig A., Engel J. The thrombospondin-like chains of cartilage oligomeric matrix protein are assembled by a five-stranded alpha-helical bundle between residues 20 and 83. FEBS Lett. 341:1994;54-58.
8. Efimov V.P., Engel J., Malashkevich V.N. Crystallization and preliminary crystallographic study of the pentamerizing domain from cartilage oligomeric matrix protein: a five-stranded alpha-helical bundle. Proteins. 24:1996;259-262.
9. Feng Y., Jefferson E.A., Goodman M. Cold denaturation of a synthetic collagen mimetic. Biopolymers. 45:1998;347-350.
10. Greenfield N.J., Hitchcock-DeGregori S.E. The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface. Biochemistry. 34:1995;16797-16805.
11. Griko Y.V., Privalov P.L., Sturtevant J.M., Venyaminov S.Y.u. Cold denaturation of staphylococcal nuclease. Proc. Natl. Acad. Sci. USA. 85:1988;3343-3347.
12. Guo Y., Bozic D., Malashkevich V.N., Kammerer R.A., Schulthess T., Engel J. All-trans retinol vitamin D and other hydrophobic compounds bind in the axial pore of the five-stranded coiled-coil domain of cartilage oligomeric matrix protein. EMBO J. 17:1998;5265-5272.
13. Handel T.M., Williams S.A., DeGrado W.F. Metal ion-dependent modulation of the dynamics of a designed protein. Science. 261:1993;879-885.
14. Jelesarov I., Durr E., Thomas R.M., Bosshard H.R. Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper). Biochemistry. 37:1998;7539-7550.
15. Kammerer R.A. Alpha-helical coiled-coil oligomerization domains in extracellular proteins. Matrix Biol. 15:1997;555-565.
16. Kitakuni E., Kuroda Y., Oobatake M., Tanaka T., Nakamura H. Thermodynamic characterization of an artificially designed amphiphilic alpha-helical peptide containing periodic prolines: observations of high thermal stability and cold denaturation. Protein Sci. 3:1994;831-837.
17. Kohn W.D., Mant C.T., Hodges R.S. Alpha-helical protein assembly motifs. J. Biol. Chem. 272:1997;2583-2586.
18. Kretschmar M., Jaenicke R. Stability of a homo-dimeric Ca(2+)-binding member of the beta gamma-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum. J. Mol. Biol. 291:1999;1147-1153.
19. Kwok S.C., Tripet B., Man J.H., Chana M.S., Lavigne P., Mant C.T., Hodges R.S. Structural cassette mutagenesis in a de novo designed protein: proof of a novel concept for examining protein folding and stability. Biopolymers. 47:1998;101-123.
20. Lacassie E., Delmas A., Meunier C., Sy D., Trudelle Y. High thermal stability and cold-denaturation of an artificial polypeptide. Int. J. Pept. Protein Res. 48:1996;249-258.
21. Lumb K.J., Kim P.S. A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry. 34:1995;8642-8648.
22. Lupas A. Coiled coils: new structures and new functions. Trends. Biochem. Sci. 21:1996;375-382.
23. Malashkevich V.N., Kammerer R.A., Efimov V.P., Schulthess T., Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? Science. 274:1996;761-765.
24. McLachlan A.D., Stewart M. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304.
25. Monera O.D., Kay C.M., Hodges R.S. Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils. Biochemistry. 33:1994;3862-3871.
26. Morgelin M., Heinegard D., Engel J., Paulsson M. Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure. J. Biol. Chem. 267:1992;6137-6141.
27. Pace N.C. Determination and analysis of urea and gaunidine chloride denaturation curves. Methods Enzymol. 131:1986;266-280.
28. Parry D.A., Steinert P.M. Intermediate filament structure. Curr. Opin. Cell. Biol. 4:1992;94-98.
29. Press W.H., Flannery B.P., Teukolsky S.A., Vetterling W.T. Numerical Recipes. 1986;Cambridge University Press, Cambridge.
30. Privalov P.L. Cold denaturation of proteins. Crit. Rev. Biochem. Mol. Biol. 25(4):1990;281-305.
31. Privalov P.L., Griko Yu V., Venyaminov S., Kutyshenko V.P. Cold denaturation of myoglobin. J. Mol. Biol. 190:1986;487-498.
32. Sodek J., Hodges R.S., Smillie L.B., Jurasek L. Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl. Acad. Sci. USA. 69:1972;3800-3804.