Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein)

Biochemical Journal

Volumn 380, Issue 2, 2004, Pages 409-417

  Bajaj, Kanika ^a   Chakshusmathi, Ghadiyaram ^a   Bachhawat Sikder, Kiran ^a   Surolia, Avadhesha ^a   Varadarajan, Raghavan ^a,b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

Author keywords

CcdB (controller of cell division or death B protein); DSC (differential scanning calorimetry); GdmCl (guanidinium chloride); Stability curve

Indexed keywords

CYTOLOGY; DIFFERENTIAL SCANNING CALORIMETRY; DIMERS; ESCHERICHIA COLI; PH EFFECTS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; TOXICITY;

DENATURANT CONCENTRATION; THERMODYNAMIC CHARACTERIZATION;

BIOCHEMISTRY;

DEATH B PROTEIN; DNA TOPOISOMERASE (ATP HYDROLYSING); GUANIDINE; MONOMER; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CALORIMETRY; CELL DIVISION; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; DIMERIZATION; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; GENETIC CODE; ISOTHERM; MELTING POINT; MOLECULAR DYNAMICS; NONHUMAN; PH; PLASMID; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; STRUCTURE ANALYSIS; THERMODYNAMICS;

BACTERIAL PROTEINS; BACTERIAL TOXINS; DIMERIZATION; ESCHERICHIA COLI PROTEINS; HEAT; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 2942740914     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031528     Document Type: Article

References (38)

1. Bernard, P., Kezdy, K. E., Van Melderen, L., Steyaert, J., Wyns, L., Pato, M. L., Higgins, P. N. and Couturier, M. (1993) The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase. J. Mol. Biol. 234, 534-541
2. Steyaert, J., Van Melderen, L., Bernard, P., Thi, M. H., Loris, R., Wyns, L and Couturier, M. (1993) Purification, circular dichroism analysis, crystallization and preliminary X-ray diffraction analysis of the F plasmid CcdB killer protein. J. Mol. Biol. 231, 513-515
3. Guzman, L. M., Belin, D., Carson, M. J. and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130
4. Van Melderen, L., Thi, M. H. D., Lecchi, P., Gottesman, S., Couturier, M. and Maurizi, M. R. (1996) ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271, 27730-27738
5. Whitaker, J. R. (1963) Determination of molecular weights of proteins by gel filtration on Sephadex. Anal. Chem. 35, 1950-1953
6. Schellman, J. A. (1987) The thermodynamic stability of proteins. Annu. Rev. Biophys. Biophys. Chem. 16, 115-137
7. Goldenberg, D. P. and Creighton, T. E. (1984) Gel electrophoresis in studies of protein conformation and folding. Anal. Biochem. 138, 1-18
8. Plotnikov, V. V., Brandts, J. M., Lin, L. N. and Brandts, J. F. (1997) A new ultrasensitive scanning calorimeter. Anal. Biochem. 250, 237-244
9. Ganesh, C., Shah, A. N., Swaminathan, C. P., Surolia, A. and Varadarajan, R. (1997) Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 36, 5020-5028
10. Loris, R., Dao-Thi, M. H., Bahassi, E. M., Van Melderen, L., Poortmans, F., Liddington, R., Couturier, M. and Wyns, L. (1999) Crystal structure of CcdB, a topoisomerase poison from E. coli. J. Mol. Biol. 285, 1667-1677
11. Dao-Thi, M. H., Messens, J., Wyns, L. and Backmann, J. (2000) The thermodynamic stability of the proteins of the ccd plasmid addiction system. J. Mol. Biol. 299, 1373-1386
12. Becktel, W. J. and Schellman, J. A. (1987) Protein stability curves. Biopolymers 26, 1859-1877
13. Privalov, P. L. (1979) Stability of proteins: small globular proteins. Adv. Protein Chem. 33, 167-241
14. Murphy, K. P. and Freire, E. (1992) Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv. Protein Chem. 43, 313-361
15. Jaenicke, R. and Lilie, H. (2000) Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53, 329-401
16. Plum, G. E. and Breslauer, K. J. (1995) Calorimetry of proteins and nucleic acids. Curr. Opin. Struct. Biol. 5, 682-690
17. 2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum. J. Mol. Biol. 291, 1147-1153
18. Blaber, S. I., Culajay, J. F., Khurana, A. and Blaber, M. (1999) Reversible thermal denaturation of human FGF-1 induced by low concentrations of guanidine hydrochloride. Biophys. J. 77, 470-477
19. Ladbury, J. E., Kishore, N., Hellinga, H. W., Wynn, R. and Sturtevant, J. M. (1994) Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. Biochemistry 33, 3688-3692
20. Zweifel, M. E. and Barrick, D. (2002) Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves. Biophys. Chem. 101-102, 221-237
21. Panse, V. G., Swaminathan, C. P., Aloor, J. J., Surolia, A. and Varadarajan, R. (2000) Unfolding thermodynamics of the tetrameric chaperone, SecB. Biochemistry 39, 2362-2369
22. Neet, K. E. and Timm, D. E. (1994) Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci. 3, 2167-2174
23. Jaenicke, R. (1987) Folding and association of proteins. Prog. Biophys. Mol. Biol. 49, 117-237
24. Backmann, J. and Schafer, G. (2001) Thermodynamic analysis of hyperthermostable oligomeric proteins. Methods Enzymol. 334, 328-342
25. Chen, J. and Smith, D. L. (2001) Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5. Protein Sci. 10, 1079-1083
26. Pineda, T., Osei, Y. D. and Churchich, J. E. (1995) Characterization of monomeric 4-aminobutyrate aminotransferase at low pH. Eur. J. Biochem. 228, 683-688
27. Mullen, C. A. and Jennings, P. A. (1996) Glycinamide ribonucleotide transformylase undergoes pH-dependent dimerization. J. Mol. Biol. 262, 746-755
28. Almassy, R. J., Janson, C. A., Kan, C. C. and Hostomska, Z. (1992) Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Proc. Natl. Acad. Sci. U.S.A. 89, 6114-6118
29. Chen, P., Schulze-Gahmen, U., Stura, E. A., Inglese, J., Johnson, D. L., Marolewski, A., Benkovic, S. J. and Wilson, I. A. (1992) Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 Å resolution. A target enzyme for chemotherapy. J. Mol. Biol. 227, 283-292
30. Inglese, J., Johnson, D. L., Shiau, A., Smith, J. M. and Benkovic, S. J. (1990) Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. Biochemistry 29, 1436-1443
31. Klein, C., Chen, P., Arevalo, J. H., Stura, E. A., Marolewski, A., Warren, M. S., Benkovic, S. J. and Wilson, I. A. (1995) Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 Å resolution. J. Mol. Biol. 249, 153-175
32. Bose, K. and Clark, A. C. (2001) Dimeric procaspase-3 unfolds via a four-state equilibrium process. Biochemistry 40, 14236-14242
33. Eftink, M. R., Helton, K. J., Beavers, A. and Ramsay, G. D. (1994) The unfolding of trp aporepressor as a function of pH: evidence for an unfolding intermediate. Biochemistry 33, 10220-10228
34. Cheng, X., Gonzalez, M. L. and Lee, J. C. (1993) Energetics of intersubunit and intrasubunit interactions of Escherichia coli adenosine cyclic 3′,5′-phosphate receptor protein. Biochemistry 32, 8130-8139
35. Asgeirsson, B., Hauksson, J. B. and Gunnarsson, G. H. (2000) Dissociation and unfolding of cold-active alkaline phosphatase from Atlantic cod in the presence of guanidinium chloride. Eur. J. Biochem. 267, 6403-6412
36. Bhatt, A. N., Prakash, K., Subramanya, H. S. and Bhakuni, V. (2002) Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase. Biochemistry 41, 12115-12123
37. Miller, S., Lesk, A. M., Janin, J. and Chothia, C. (1987) The accessible surface area and stability of oligomeric proteins. Nature (London) 328, 834-836
38. Kampranis, S. C., Howells, A. J. and Maxwell, A. (1999) The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes. J. Mol. Biol. 293, 733-744