Structural changes and interactions involved in the Ca2+-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11

Applied and Environmental Microbiology

Volumn 66, Issue 5, 2000, Pages 2021-2028

  Exterkate, Fred A ^a  

^a NIZO FOOD RESEARCH   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; SUCROSE;

ARTICLE; BACTERIAL MEMBRANE; BINDING SITE; CONTROLLED STUDY; ELECTRIC POTENTIAL; ENZYME STABILITY; HYDROPHOBICITY; LACTOCOCCUS LACTIS; NONHUMAN; PROTEIN DEGRADATION;

BINDING SITES; CALCIUM; CELL MEMBRANE; ELECTROSTATICS; ENDOPEPTIDASES; ENZYME STABILITY; KINETICS; LACTOCOCCUS LACTIS; SERINE ENDOPEPTIDASES; SUCROSE;

BACTERIA (MICROORGANISMS); LACTOCOCCUS; LACTOCOCCUS LACTIS; LACTOCOCCUS LACTIS SUBSP. CREMORIS; POSIBACTERIA; STREPTOCOCCUS;

EID: 0034020319     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.5.2021-2028.2000     Document Type: Article

References (26)

1. Baankreis, R., S. van Schalkwijk, A. C. Alting, and F. A. Exterkate. 1995. The occurrence of two intracellular oligoendopeptidases in Lactococcus lactis and their significance for peptide conversion in cheese. Appl. Microhiol. Biotechnol. 44:386-392.
2. Bajorath, J., S. Raghunathan, W. Hinrichs, and W. Saenger. 1989. Long-range structural changes in proteinase K triggered by calcium ion removal. Nature 337:481-484.
3. Bruinenberg, P. G., P. Vos, and W. M. de Vos. 1992. Proteinase overproduction in Lactococcus lactis strains: regulation and effect on growth and acidification in milk. Appl. Environ. Microhiol. 58:78-84.
4. Butler, S. L., and J. J. Falke. 1996. Effects of protein stabilizing agents on thermal backbone motions: a disulfide trapping study. Biochemistry 35:10595-10600.
5. Coolbear, T., J. R. Reid, and G. G. Pritchard. 1992. Stability and specificity of the cell-wall-associated proteinase from Lactococcus lactis subsp. cremoris H2 released by treatment with lysozyme in the presence of calcium. Appl. Environ. Microbiol. 58:3263-3270.
6. Dill, K. A. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
7. Exterkate, F. A. 1995. The lactococcal cell envelope proteinases: differences, Ca-binding effects and role in cheese ripening. Int. Dairy J. 5:995-1018.
8. Exterkate, F. A., and G. J. C. M. de Veer. 1985. Partial isolation of and degradation of caseins by cell wall proteinases of Streptococcus cremoris HP. Appl. Environ. Microbiol. 49:328-332.
9. 1 and its relationship with the catalytically different cell wall proteinase PI/PH of strain HP. Syst. Appl. Microbiol. 11:108-115.
10. Exterkate, F. A., A. C. Alting, and P. G. Bruinenberg. 1993. Diversity of cell-envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region. Appl. Environ. Microbiol. 59:3640-3647.
11. Exterkate, F. A., and A. C. Alting. 1999. Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase. Appl. Environ. Microbiol. 65:1390-1396.
12. Gekko, K., and S. N. Timasheff. 1981. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry 20:4677-4686.
13. Genov, N., B. Filippi, P. Dolashka, K. S. Wilson, and Ch. Betzel. 1995. Stability of subtilisins and related proteinases (subtilases). Int. J. Peptide Prot. Res. 45:391-400.
14. Kunji, E. R. S., I. Mierau, A. Hagting, B. Poolman, and W. N. Konings. 1996. The proteolytic systems of lactic acid bacteria, p. 187-221. In G. Venema, J. H. J. Huis in't Veld, and J. Hugenholtz, (ed.), Lactic acid bacteria: genetics, metabolism, and applications. Kluvver Academic Publishers, Dordrecht, The Netherlands.
15. Leberman, R., and A. K. Soper. 1995. Effect of high salt concentrations on water structure. Nature 378:364-366.
16. Lee, J. C., and S. N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256:7193-7201.
17. Navarre, W. W., and O. Schneewind. 1994. Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol. Microbiol. 14:115-121.
18. Pritchard, G. G., and T. Coolbear. 1993. The physiology and biochemistry of the proteolytic system in lactic acid bacteria. FEMS Microbiol. Rev. 12:179-206.
19. Sandberg, W. S., and T. C. Terwilliger. 1989. Influence of interior packing and hydrophobicity on the stability of a protein. Science 245:54-57.
20. Schneewind, O., D. Mihaylova-Petkov, and P. Model. 1993. Cell wall sorting signals in surface proteins of gram-positive bacteria. EMBO J. 12:4803-4811.
21. Siezen, R. J. 1999. Multidomain, cell-envelope proteinases of lactic acid bacteria. Antonie Leeuwenhoek 76:139-155.
22. Siezen, R. J., W. M. de Vos, A. M. Leunissen, and B. W. Dijksta. 1991. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Prot. Eng. 4:717-737.
23. Timasheff, S. N. 1993. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22:67-97.
24. s1, β- and κ-casein. Appl. Environ. Microbiol. 52:1162-1166.
25. Von Hippel, P. H., and T. Schleich. 1969. The effects of neutral salts on the structure and conformational stability of macromolecules in solution, p. 417-574. In S. N. Timasheff and G. D. Fasman (ed.), Structure and stability of biological molecules. Marcel Dekker, Inc., New York, N.Y.
26. Vos, P., G. Simons, R. J. Siezen, and W. M. de Vos. 1989. Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase. J. Biol. Chem. 264:13579-13585.