Stability of a homo-dimeric Ca2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum

Journal of Molecular Biology

Volumn 291, Issue 5, 1999, Pages 1147-1153

  Kretschmar, Michael ^a   Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Calcium binding; Differential scanning calorimetry; Dimer; Spherulin; crystallins

Indexed keywords

BETA CRYSTALLIN; CALCIUM BINDING PROTEIN; CALCIUM ION; CYSTEINE; GUANIDINE; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; DIMERIZATION; ENTHALPY; FLUORESCENCE SPECTROSCOPY; MOLECULAR MODEL; NONHUMAN; PHYSARUM POLYCEPHALUM; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN STABILITY;

CHONDROMYCES; PHYSARUM POLYCEPHALUM; STAPHYLOCOCCUS PHAGE 3A;

EID: 0033520346     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3037     Document Type: Article

References (27)

1. Baldwin R. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl Acad. Sci. USA. 83:1986;8069-8072.
2. Blundell T., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., Wistow G. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature. 289:1981;771-777.
3. Chiti F., van Nuland A. J., Taddei N., Magherini F., Stefani M., Ramponi G., Dobson M. Conformational stability of muscle acylphophatase: the role of temperature, denaturant concentration and pH. Biochemistry. 37:1998;1447-1455.
4. Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202:1991;715-728.
5. Jaenicke R. Stability and folding of domain proteins. Prog. Biophys. Mol. Biol. 71:1999;155-241.
6. Karantza V., Baxevanis A. D., Freire E., Moudrianakis E. N. Thermodynamic studies of the core-histones: ionic strength and pH dependence of H2A-H2B dimer stability. Biochemistry. 34:1995;5988-5996.
7. Kretschmar M., Mayr E.-M., Jaenicke R. Homo-dimeric spherulin 3a: a single-domain member of the βγ-crystallin superfamily. Biol. Chem. 380:1999a;89-94.
8. 2+binding. J. Mol. Biol. 289:1999b;701-705.
9. Livingstone J., Spolar R., Record T. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry. 30:1991;4237-4244.
10. Marky L. A., Breslauer K. J. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers. 26:1987;1601-1620.
11. Mayr E.-M., Jaenicke R., Glockshuber R. Domain interactions and connecting peptides in lens crystallins. J. Mol. Biol. 235:1994;84-88.
12. Mayr E. M., Jaenicke R., Glockshuber R. The domains in γB-crystal lin: identical fold-different stabilities. J. Mol. Biol. 269:1997;260-269.
13. Myers J. K., Pace C. N., Scholtz J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
14. Palme S., Slingsby C., Jaenicke R. Mutational analysis of hydrophobic domain interactions in γB-crystallin from bovine eye lens. Protein Sci. 6:1997;1529-1536.
15. Pfeil P., Gesierich U., Kleemann G. R., Sterner R. Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water. J. Mol. Biol. 272:1997;591-596.
16. Privalov G. P., Kavina V., Freire E., Privalov P. L. Precise scanning calorimeter for study of thermal properties of biological macromolecules in dilute solutions. Anal. Biochem. 232:1995;79-85.
17. Privalov P. L. Stability of proteins: small globular proteins. Advan. Protein Chem. 33:1979;167-241.
18. 2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype γ-crystallin fold in aqueous solution. J. Mol. Biol. 272:1997;645-655.
19. Schellman J. A. The thermodynamic stability of proteins. Annu. Rev. Biophys. Biophys. Chem. 16:1987;115-137.
20. Schlunegger M. P., Bennett M. J., Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Advan. Protein Chem. 50:1997;61-122.
21. Steif C., Weber P., Hinz H. J. Subunit interactions provide a significant contribution to the stability of the dimeric four-α-helical-bundle protein ROP. Biochemistry. 32:1993;3867-3876.
22. Wenk M. Protein S aus Myxococcus xanthus und seine isolierten Domänen: Stabilität, Wechselwirkungen, Faltung und Struktur. 1999;Dissertation, University of Regensburg.
23. Wenk M., Mayr E. M. Myxococcus xanthus spore coat protein S, a stress-induced member of the βγ-crystallin superfamily, gains stability from binding of calcium ions. Eur. J. Biochem. 225:1998;604-610.
24. Wenk M., Baumgartner R., Holak T. A., Huber R., Jaenicke R., Mayr E. M. The domains of protein S from Myxococcus xanthus: structure, stability and interactions. J. Mol. Biol. 286:1999;1533-1545.
25. Wieligmann K., Mayr E. M., Jaenicke R. Folding and selfassembly of domains of βB2-crystallin from rat lens. J. Mol. Biol. 286:1999;989-994.
26. Wistow G. Evolution of a protein superfamily: relationship between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30:1990;40-145.
27. Zhou Y., Hall C. K., Karplus M. The calorimetric criterion for a two-state process revisited. Protein Sci. 8:1999;1064-1074.