Contribution of Protein-Surface Ion Pairs of a Hyperthermophilic Protein on Thermal and Thermodynamic Stability

Journal of Bioscience and Bioengineering

Volumn 97, Issue 1, 2004, Pages 75-77

  Shiraki, Kentaro ^a   Nishikori, Shingo ^a   Fujiwara, Shinsuke ^b   Imanaka, Tadayuki ^c   Takagi, Masahiro ^a  

^a JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b KWANSEI GAKUIN UNIVERSITY   (Japan)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

Archaea; Ion pair; Protein folding; Thermal stability; Thermodynamic stability

Indexed keywords

DNA; FREE ENERGY; PROTEINS; THERMODYNAMIC STABILITY;

ION PAIRS; PROTEIN SURFACE;

BIOMEDICAL ENGINEERING;

PROTEIN; SODIUM CHLORIDE;

ARTICLE; CONTROLLED STUDY; NONHUMAN; PH; SURFACE PROPERTY; TEMPERATURE; THERMOCOCCUS; THERMOCOCCUS KODAKARUENSIS; THERMODYNAMICS;

ARCHAEA; THERMOCOCCUS; THERMOCOCCUS KODAKARAENSIS;

EID: 0442329212     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(04)70169-3     Document Type: Review

References (24)

1. Yip, K. S., Britton, K. L., Stillman, T. J., Lebbink, J., de Vos, W. M., Robb, F. T., Vetriani, C., Maeder, D., and Rice, D.W.: Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family. Eur. J. Biochem., 255, 336-346 (1998).
2. Hennig, M., Darimont, B., Sterner, R., Kirschner, K., and Jansonius, J. N.: 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure, 3, 1295-1306 (1995).
3. Jaenicke, R., Schurig, H., Beaucamp, N., and Ostendorp, R.: Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv. Protein Chem., 48, 181-269 (1996).
4. Lim, J., Yu, Y. G., Han, Y. S., Cho, S., Ahn, B., Kim, S., and Cho, Y.: The crystal structure of an Fe-superoxide dismutase from the hyperthemophile Aquifex pyrophilus at 1.9 Å resolution: structural basis for thermostability. J. Mol. Biol., 270, 259-274 (1997).
5. Dao-pin, S., Sauer, U., Nicholson, H., and Matthews, B. W.: Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry, 30, 7142-7153 (1991).
6. Sali, D., Bycroft, M., and Fersht, A. R.: Surface electrostatic interactions contribute little stability of barnase. J. Mol. Biol., 220, 779-788 (1991).
7. Zhou, N. E., Kay, C. M., and Hodges, R. S.: The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng., 7, 1365-1372 (1994).
8. Kammerer, R. A., Jaravine, V. A., Frank, S., Schulthess, T., Landwehr, R., Lustig, A., Garcia-Echeverria, C., Alexandrescu, A. T., Engel, J., and Steinmetz, M. O.: An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper. J. Biol. Chem., 276, 13685-13688 (2001).
9. Lounnas, V. and Wade, R. C.: Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry, 36, 5402-5417 (1997).
10. 6-methylguanine-DNA methyltransferase from the hyperthermophilic archaeon Pyrococcus sp. KOD1: a thermostable repair enzyme. Mol. Gen. Genet., 258, 69-77 (1998).
11. 6-methylguanine-DNA methyltransferase. J. Mol. Biol., 292, 707-716 (1999).
12. Shiraki, K., Nishikori, S., Fujiwara, S., Hashimoto, H., Kai, Y., Takagi, M., and Imanaka, T.: Comparative analyses of the conformational stability between a hyperthermophilic protein and its mesophilic counterpart. Eur. J. Biochem., 268, 4144-4150 (2001).
13. Shiraki, K., Fujiwara, S., Takagi, M., and Imanaka, T.: Conformational stability of a hyperthermophilic protein in alcohol and other denatured conditions. Electrochemistry, 69, 949-952 (2001).
14. Hendsch, Z. S. and Tidor, B.: Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci., 3, 211-226 (1994).
15. Zhou, H. X.: Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding. Biophys. J., 83, 3126-3133 (2002).
16. Perutz, M. F. and Raidt, H.: Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglebin A2. Nature, 255, 256-259 (1975).
17. Elcock, A. H.: The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol., 284, 489-502 (1998).
18. Zhou, H. X.: Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding. Biophys. J., 83, 3126-3133 (2002).
19. Hollien, J. and Marqusee, S.: A thermodynamic comparison of mesophilic and thermophilic ribonucreases. Biochemistry, 38, 3831-3836 (1999).
20. Deutscham, W. A. and Dahlquist, F. W.: Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima. Biochemistry, 40, 13107-13113 (2001).
21. Motono, C., Oshima, T., and Yamagishi, A.: High thermal stability of 2-isopropylmalate dehydrogenase from Thermus thermophilus resulting from low ΔΔCp of unfolding. Protein Eng., 14, 961-966 (2001).
22. Knapp, S., Karshikoff, A., Berndt, K. D., Christova, P., Atanasov, B., and Ladenstein, R.: Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus. J. Mol. Biol., 264, 1132-1144 (1996).
23. Knapp, S., Mattson, P. T., Christva, P., Berndt, K. D., Karshikoff, A., Vihinen, M., Smith, C. I., and Ladenstein, R.: Thermal unfolding of small proteins with SH3 domain folding pattern. Proteins, 31, 309-319 (1998).
24. Filimonov, V. V., Azuaga, A. I., Viguera, A. R., Serrano, L., and Mateo, P. L.: A thermodynamic analysis of a family of small globular proteins: SH3 domains. Biophys. Chem., 77, 195-208 (1999).