Calcium triggers the refolding of Bacillus subtilis chitosanase

Biochemical Journal

Volumn 369, Issue 3, 2003, Pages 731-738

  Colomer Pallas, Anne ^a   Pereira, Yannick ^a   Petit Glatron, Marie Françoise ^a   Chambert, Régis ^a  

^a INSTITUT JACQUES MONOD   (France)

Author keywords

Exocellular protein; Reversible folding; Thermal unfolding; Urea denaturation

Indexed keywords

CALCIUM; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; POSITIVE IONS; TITRATION;

PROTEOLYSIS;

PROTEINS;

CALCIUM; CHITOSANASE;

ARTICLE; BACILLUS SUBTILIS; BINDING AFFINITY; BINDING SITE; CONCENTRATION (PARAMETERS); DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; TITRIMETRY;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CALCIUM; CELL DIVISION; DURAPATITE; ENZYME STABILITY; FLUORESCENCE; GLYCOSIDE HYDROLASES; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TITRIMETRY; UREA;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 0037325725     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021459     Document Type: Article

References (22)

1. Eilers, M. and Schatz, G. (1988) Protein unfolding and the energetics of protein translocation across biological membranes. Cell 52, 481-483
2. Van Wely, K. H., Swaving, J., Freudl, R. and Driessen, A. J. (2001) Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol. Rev. 25, 437-454
3. Otha, Y., Hojo, H., Aimoto, S., Kobayashi, T., Zhu, X., Jordan, F. and Inouye, M. (1991) Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide. Mol. Microbiol. 5, 1507-1510
4. Jacobs, M., Anderson, J. B., Kontinen, V. and Sarvas, M. (1993) Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences. Mol. Microbiol. 8, 957-966
5. Doyle, R. (1989) How cell walls of Gram-positive bacteria interact with metal ions. In Metal Ions and Bacteria (Beveridge, T. J. and Doyle, R. J., eds.), pp. 275-293, John Wiley and Sons, New York
6. Chambert, R. and Petit-Glatron, M. F. (1999) Anionic polymers of Bacillus subtilis cell wall modulate the folding rate of secreted proteins. FEMS Lett. 179, 43-47
7. Chambert, R., Haddaoui, E. A. and Petit-Glatron, M. F. (1995) Bacillus subtilis levansucrase: the efficiency of the second stage of secretion is modulated by external effectors assisting folding. Microbiology 141, 997-1005
8. Haddaoui, E. A., Leloup, L., Petit-Glatron, M. F. and Chambert, R. (1997) Characterization of a stable intermediate trapped during reversible refolding of Bacillus subtilis alpha-amylase. Eur. J. Biochem. 249, 505-509
9. Rivas, L. A., Parro, V., Moreno-Paz, M. and Mellado, R. P. (2000) The Bacillus subtilis 168 csn gene encodes a chitosanase with similar properties to a Streptomycss enzyme. Microbiology 146, 2929-2936
10. Pereira, Y., Chambert, R., Leloup, L., Daguer, J. P. and Petit-Glatron, M. F. (2001) Transcripts of the genes sacB, amyE, sacC and csn expressed in Bacillus subtilis under the control of the 5′ untranslated sacR region display ditferent stabilities that can be modulated. Microbiology 147, 1331-1341
11. Honda, Y., Fukamizo, T., Okajima, T., Goto, S., Boucher, I. and Brzezinski, R. (1999) Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. Biochim. Biophys. Acta 1429, 365-376
12. Chambert, R. and Petit-Glatron, M. F. (1984) Hyperproduction of exocellular levansucrase by Bacillus subtilis: examination of the phenotype of a sacUh strain. J. Gen. Microbiol. 130, 3143-3152
13. Uchida, Y. and Ohtakara, A. (1988) Chitosanase from Bacillus species. Methods Enzymol. 161, 501-505
14. Miller, G. L. (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31, 426-428
15. Parro, V., San Roman, M., Galindo, I., Bolotin, A., Sorokin, A. and Mellado, R. P. (1997) A 23911 bp region of the Bacillus subtilis genome comprising genes located upstream and downstream of the lev operon. Microbiology 143, 1321-1326
16. Somashekar, D. and Richard, J. (1996) Chitosanases-properties and applications: a review. Bioresour. Technol. 55, 35-45
17. Yang, J. T., Wu, S. C. and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269
18. Tanford, C. (1968) Protein denaturation. Adv. Protein Chem. 23, 121-282
19. Pace, C. N. and Shaw, K. L. (2000) Linear extrapolation method of analyzing solvent denaturation curves. Proteins 4, 1-7
20. Pantoliano, M. W., Whitlow, M., Wood, J. F., Rollence, M. L., Finzel, B. C., Gilliland, G. L., Poulos, T. L. and Bryan, P. N. (1988) The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry 27, 8311-8317
21. Reid, R. E., Gariepy, J., Saund, A. K. and Hodges, R. S. (1981) Calcium-induced protein folding. Structure-affinity relationships in synthetic analogs of the helix-loop-helix calcium binding unit. J. Biol. Chem. 256, 2742-2751
22. Garnier, J. (1977) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120