Skip to main content
SpringerLink
Log in

Intracellular Peptidoglycan Hydrolases of the Bacterium Xanthomonas campestris XL-1

  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

A system of intracellular peptidoglycan hydrolases of Xanthomonas campestris XL-1 comprises about 10 enzymes of different localization and substrate specificity. Seven enzymes (A1-A7) are localized in cytosol, one enzyme (A8) in periplasm, and two enzymes (A9, A10) were found in the fraction of cell walls and membranes. While the culture is entering the logarithmic growth stage from the stationary stage, a change occurs in the activity of the cytosolic enzymes: A1 significantly increases, and A5 and A6 decrease. The spectrum of cytosolic enzymes also depends on the growth medium composition. The enzyme A7 present in cells secreting extracellular enzymes (medium 5/5) was not found in non-secreting cells (LB medium). Unlike extracellular enzymes, intracellular peptidoglycan hydrolases are primarily acidic proteins. The data indicate that the system of intracellular peptidoglycan hydrolases of X. campestris is under complex and strict regulation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

REFERENCES

  1. Shockman, G. D., and Holtje, J.-V. (1994) in New Comprehensive Biochemistry: Bacterial Cell Wall (Ghusen, J. M., and Hakenbeck, R., eds.) Elsevier Sciense B. V., Amsterdam, The Netherlands, pp. 131-165.

    Google Scholar 

  2. Stepnaya, O. A., Ledova, L. A., and Kulaev, I. S. (1999) Usp. Biol. Khim., 39, 327-354.

    Google Scholar 

  3. Murao, S., and Takahara, G. (1973) Agr. Biol. Chem., 37, 2671-2673.

    Google Scholar 

  4. Robinson, J. M., Reating, M. S., and Sloan, G. L. (1980) J. Gen. Microbiol., 118, 529-533.

    Google Scholar 

  5. Burge, M., and Pattee, P. A. (1967) J. Bacteriol., 93, 860-865.

    Google Scholar 

  6. Ghusen, J. M., Dierickz, L., Coette, J., Leyh Bouille, M., Guinand, M., and Campbell, J. M. (1969) Biochemistry, 8, 213-222.

    Google Scholar 

  7. Stepnaya, O. A., Severin, A. I., and Kulaev, I. S. (1986) Biokhimiya, 51, 909-915.

    Google Scholar 

  8. Stepnaya, O. A., Severin, A. I., Kudryavtseva, A. I., Krupyanko, V. I., Kozlovskii, A. G., and Kulaev, I. S. (1992) Prikl. Biokhim. Mikrobiol., 28, 666-673.

    Google Scholar 

  9. Stepnaya, O. A., Begunova, E. A., Tsfasman, I. M., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 471-476.

    Google Scholar 

  10. Stepnaya, O. A., Begunova, E. A., Tsfasman, I. M., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 477-482.

    Google Scholar 

  11. Tsfasman, I. M., Stepnaya, O. A., Bazhanova, N. V., and Kulaev, I. S. (2000) Biochemistry (Moscow), 65, 1036-1040.

    Google Scholar 

  12. Davis, R. W., Botstein, D., and Roth, J. (1980) Advanced Bacterial Genetics. Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.

    Google Scholar 

  13. Nossal, N. G., and Heppel, L. A. (1966) J. Biol. Chem., 241, 3055-3062.

    Google Scholar 

  14. Brown, W. C. (1973) Appl. Microbiol., 25, 295-300.

    Google Scholar 

  15. Mett, H., Keck, W., Funk, A., and Schwarz, U. (1980) J. Bacteriol., 144, 45-52.

    Google Scholar 

  16. Ornstein, L., and Devis, B. J. (1964) Ann. N. Y. Acad. Sci. USA, 121, 321-403.

    Google Scholar 

  17. Reisfeld, R. A., Lewis, U. J., and Williams, D. E. (1962) Nature, 195, 281.

    Google Scholar 

  18. Kornberg, A., and Horecker, B. L. (1955) in Methods in Enzymology (Colowick, S. P., and Kaplan, N. O., eds.) Academic Press, New York, pp. 323-325.

    Google Scholar 

  19. Kornberg, A. (1966) in Methods in Enzymology (Colowick, S. P., and Kaplan, N. O., eds.) Academic Press, New York, p. 441.

    Google Scholar 

  20. Neu, H. C., and Heppel, L. A. (1965) J. Biol. Chem., 240, 3685-3692.

    Google Scholar 

  21. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem., 193, 265-275.

    Google Scholar 

  22. Stepnaya, O. A., Tsfasman, I. M., Ledova, L. A., Petrikevich, S. B., Begunova, E. A., and Kulaev, I. S. (1996) Biochemistry (Moscow), 65, 339-344.

    Google Scholar 

  23. Deutsch, J. (1983) in Methods of Enzymatic Analysis (Bergmeyer, H. U., ed.) Vol. 3, Verlag Chemie, Florida, pp. 190-197.

    Google Scholar 

  24. Vassault, A. (1983) in Methods of Enzymatic Analysis (Bergmeyer, H. U., ed.) Vol. 3, Verlag Chemie, Florida, pp. 118-126.

    Google Scholar 

  25. Holtje, J.-V., and Tuomanen, E. I. (1991) J. Gen. Microbiol., 137, 441-454.

    Google Scholar 

  26. Engel, A., Kazemier, B., and Keck, W. (1991) J. Bacteriol., 173, 6773-6782.

    Google Scholar 

  27. Walderich, B., and Holtje, J.-V. (1991) J. Bacteriol., 173, 5668-5676.

    Google Scholar 

  28. Diaz, E., Garcia, E., Ascaso, C., Mondez, E., Lopez, R., and Garcia, J. L. (1989) J. Biol. Chem., 264, 1238-1244.

    Google Scholar 

  29. Zagotta, M. T., and Wilson, D. B. (1990) J. Bacteriol., 172, 912-921.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Russian Academy of Sciences, pr. Nauki 5, Institute of Biochemistry and Physiology of Microorganisms, Pushchino, Moscow Region, 142290, Russia

    B. V. Sitkin, I. M. Tsfasman & O. A. Stepnaya

Authors
  1. B. V. Sitkin
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. I. M. Tsfasman
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. O. A. Stepnaya
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. I. S. Kulaev
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sitkin, B.V., Tsfasman, I.M., Stepnaya, O.A. et al. Intracellular Peptidoglycan Hydrolases of the Bacterium Xanthomonas campestris XL-1. Biochemistry (Moscow) 68, 458–463 (2003). https://doi.org/10.1023/A:1023660215815

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1023660215815

Search

Navigation