Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: Strategies of protein stabilization

FEMS Microbiology Reviews

Volumn 18, Issue 2-3, 1996, Pages 215-224

  Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Glyceraldehyde 3 phosphate dehydrogenase; Protein stability; Thermal stress; Thermotoga maritima

Indexed keywords

ENZYME; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

CONFERENCE PAPER; ENZYME STABILITY; HEAT STRESS; NONHUMAN; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOPHILIC BACTERIUM;

BACTERIA (MICROORGANISMS); THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0029922615     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/0168-6445(96)00013-7     Document Type: Conference Paper

References (33)

1. Jaenicke, R. (1991) Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715-728.
2. Stetter, K.O. (1993) The lesson of archeaebacteria. In: Early Life on Earth (Bengtson, S., Ed.), Nobel Symp. 84, 101-109.
3. de Grado, W.F. (1988) Design of peptides and proteins. Adv. Protein Chem. 39, 51-124.
4. Wetlaufer, D.B. (1980) Practical consequences of protein folding mechanisms. In: Protein Folding (Jaenicke, R., Ed.), pp. 323-329, Elsevier/North-Holland Biomedical Press, Amsterdam, New York.
5. Schumann, J., Wrba, A., Jaenicke, R. and Stetter, K.O. (1991) Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima. FEBS Lett. 282, 122-126.
6. Jaenicke, R., Schurig, H., Beaucamp, N. and Ostendorp, R. (1996) Structure and stability of ultrastable proteins: Glycolytic enzymes from Thermotoga maritima. Adv. Protein Chem., in press.
7. Jaenicke, R. (1994) Studies on hyperstable proteins: Crystallins from the eye lens and enzymes from thermophilic bacteria. In: Statistical Mechanics, Protein Structure and Protein-ligand Interactions (Doniach, S., Ed.), pp. 49-62, Plenum Press, New York.
8. Somero, G.N. (1992) Adaptations to high hydrostatic pressure. Annu. Rev. Physiol., 54, 557-577.
9. Jaenicke, R. (1981) Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10, 1-67.
10. Shoichet, B.K., Baase, W.A., Kuroki, R. and Matthews, B.W. (1995) A relationship between protein stability and protein function. Proc. Natl. Acad. Sci. USA 92, 452-456.
11. Jaenicke, R. (1995) Protein folding and association: Significance of in vitro studies for self-organization and targeting in the cell. Curr. Topics Cell. Regul. 34, 209-314.
12. Böhm, G. and Jaenicke, R. (1994) On the relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Peptide Protein Res. 43, 97-106.
13. Matthews, B.W. (1995) Studies on protein stability with T4 lysozyme. Adv. Protein Chem. 46, 249-278.
14. Harris. J.I. and Waters. M. (1975) Glyceraldehyde-3-phosphate dehydrogenase. In: The Enzymes, 3rd Edn. (Boyer, P.D., Ed.), Vol. 13, pp. 1-50, Academic Press, New York.
15. Wrba, A., Schweiger, A., Schultes, V., Jaenicke, R. and Závodszky, P. (1990) GAPDH from the extreme thermophilic eubacterium Thermotoga maritima. Biochemistry 29, 7584-7592.
16. Rehaber, V. and Jaenicke, R. (1992) Stability and reconstitution of GAPDH from the hyperthermophilic eubacterium Thermotoga maritima. J. Biol. Chem. 267, 10999-11006.
17. Argos, P., Rossmann, M.G., Grau, U.M., Zuber, H., Frank, G. and Tratschin, J.D. (1979) Thermal stability and protein structure. Biochemistry 18, 5698-5703.
18. Schultes, V., Deutzmann, R. and Jaenicke, R. (1990) Complete amino acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. Eur. J. Biochem. 192, 25-31.
19. Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. and Jaenicke, R. (1995) The crystal structure of holo-GAPDH from the hyperthermophilic bacterium Thermotoga mar. at 2.5 Å resolution. J. Mol. Biol. 246, 511-521.
20. 2. Nature (Lond.) 255, 256-259.
21. Tomschy, A., Glockshuber, R. and Jaenicke, R. (1993) Cloning and expression of GAPDH from the hyperthermophilic bacterium Thermotoga maritima. Eur. J. Biochem., 214, 43-50.
22. Tomschy, A. (1993) Klonierung, Expression und Charakterisierung der hyperthermophilen GAPDH aus Thermotoga maritima und ihrer Koenzymbindenden Domäne. Dissertation, Universität Regensburg.
23. Tomschy, A., Böhm, G. and Jaenicke, R. (1994) Effect of central and peripheral ion-pairs on the thermal stability of GAPDH from Thermotoga maritima. Protein Engineering 7, 1471-1478.
24. Skarzynski, T., Moody. P.C.E. and Wonnacot, A.J. (1987) Structure of holo-GAPDH from B. st. at 1.8 Å resolution. J. Mol. Biol. 193, 171-187.
25. Opitz, U., Rudolph, R., Jaenicke, R., Ericsson, L. and Neurath, H. (1987) Proteolytic dimers of porcine LDH: Characterization, folding and reconstitution of the truncated and nicked polypeptide chain. Biochemistry 26, 1399-1406.
26. Mayr, E.-M., Jaenicke, R. and Glockshuber, R. (1994) Domain interactions and connecting peptides in lens crystallins. J. Mol. Biol. 235, 84-88.
27. Jecht, M., Tomschy, A., Kirschner, K. and Jaenicke, R. (1994) Autonomous folding of the excised coenzyme-binding domain of GAPDH from Thermotoga maritima. Protein Sci. 3, 411-418.
28. Jaenicke, R. (1987) Folding and association of proteins. Progr. Biophys. Mol. Biol. 49, 117-237.
29. Bartholmes, P. and Jaenicke, R. (1978) Reassociation and reactivation of yeast GAPDH after dissociation in the presence of ATP. Eur. J. Biochem. 87, 563-567.
30. Krebs, H., Rudolph, R. and Jaenicke, R. (1979) Influence of coenzyme on the refolding and reassociation in vitro of GAPDH from yeast. Eur. J. Biochem. 100, 359-364.
31. Jaenicke, R., Krebs, H., Rudolph, R. and Woenckhaus, C. (1980) Rate enhancement of reconstitution of GAPDH by a covalently bound coenzyme analog. Proc. Natl. Acad. Sci. USA 77, 1966-1969.
32. Schultes, V. and Jaenicke, R. (1991) Folding intermediates of hyperthermophilic GAPDH from Thermotoga maritima are trapped at low temperature. FEBS Lett. 290, 235-238.
33. Rehaber, V. and Jaenicke, R. (1993) The low-temperature folding intermediate of hyperthermophilic GAPDH from Thermotoga maritima shows a native-like cooperative unfolding transition. FEBS Lett. 317, 163-166.