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. 1982 Aug;151(2):756–763. doi: 10.1128/jb.151.2.756-763.1982

Periplasmic enzymes in Bdellovibrio bacteriovorus and Bdellovibrio stolpii.

D A Odelson, M A Patterson, R B Hespell
PMCID: PMC220322  PMID: 6124531

Abstract

When cells of either Bdellovibrio bacteriovorus 109J or Bdellovibrio stolpii UKi2 were subjected to osmotic shock by treatment with sucrose-EDTA and MgCl2 solutions, only trace amounts of proteins or enzyme activities were released into the shock fluid. In contrast, when nongrowing cells were converted to motile, osmotically stable, peptidoglycan-free spheroplasts by penicillin treatment, numerous proteins were released into the suspending fluid. For both species, this suspending fluid contained substantial levels of 5'-nucleotidase, purine phosphorylase, and deoxyribose-phosphate aldolase. Penicillin treatment also released aminoendopeptidase N from B. bacteriovorus, but not from B. stolpii. Penicillin treatment did not cause release of cytoplasmic enzymes such as malate dehydrogenase. The data indicated that bdellovibrios possess periplasmic enzymes or peripheral enzymes associated with the cell wall complex. During intraperiplasmic bdellovibrio growth, periplasmic and cytoplasmic enzymes of the Escherichia coli substrate cell were not released upon formation of the spherical bdelloplast during bdellovibrio penetration. Most of the E. coli enzymes were retained within the bdelloplast until later in the growth cycle, when they became inactivated or released into the suspending buffer or both.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abram D., Castro e Melo J., Chou D. Penetration of Bdellovibrio bacteriovorus into host cells. J Bacteriol. 1974 May;118(2):663–680. doi: 10.1128/jb.118.2.663-680.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beacham I. R. Periplasmic enzymes in gram-negative bacteria. Int J Biochem. 1979;10(11):877–883. doi: 10.1016/0020-711x(79)90117-4. [DOI] [PubMed] [Google Scholar]
  3. Carls R. A., Hanson R. S. Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1971 Jun;106(3):848–855. doi: 10.1128/jb.106.3.848-855.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cerny G., Teuber M. Differential release of periplasmic versus cytoplasmic enzymes from Escherichia coli B by polymixin B. Arch Mikrobiol. 1971;78(2):166–179. doi: 10.1007/BF00424873. [DOI] [PubMed] [Google Scholar]
  5. Hespell R. B., Canale-Parola E. Carbohydrate metabolism in Spirochaeta stenostrepta. J Bacteriol. 1970 Jul;103(1):216–226. doi: 10.1128/jb.103.1.216-226.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hespell R. B. Glycolytic and tricarboxylic acid cycle enzyme activities during intraperiplasmic growth of Bdellovibrio bacteriovorus on Escherichia coli. J Bacteriol. 1976 Nov;128(2):677–680. doi: 10.1128/jb.128.2.677-680.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hespell R. B. Intraperiplasmic growth of Bdellovibrio bacteriovorus on heat-treated Escherichia coli. J Bacteriol. 1978 Mar;133(3):1156–1162. doi: 10.1128/jb.133.3.1156-1162.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hespell R. B., Mertens M. Effects of nuclei acid compounds on viability and cell composition of Bdellovibrio bacteriovorus during starvation. Arch Microbiol. 1978 Feb;116(2):151–159. doi: 10.1007/BF00406030. [DOI] [PubMed] [Google Scholar]
  9. Hespell R. B., Miozzari G. F., Rittenberg S. C. Ribonucleic acid destruction and synthesis during intraperiplasmic growth of Bdellovibrio bacteriovorus. J Bacteriol. 1975 Aug;123(2):481–491. doi: 10.1128/jb.123.2.481-491.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hespell R. B., Odelson D. A. Metabolism of RNA-ribose by Bdellovibrio bacteriovorus during intraperiplasmic growth on Escherichia coli. J Bacteriol. 1978 Dec;136(3):936–946. doi: 10.1128/jb.136.3.936-946.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hespell R. B., Rosson R. A., Thomashow M. F., Rittenberg S. C. Respiration of Bdellovibrio bacteriovorus strain 109J and its energy substrates for intraperiplasmic growth. J Bacteriol. 1973 Mar;113(3):1280–1288. doi: 10.1128/jb.113.3.1280-1288.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lane L. C. A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Anal Biochem. 1978 Jun 1;86(2):655–664. doi: 10.1016/0003-2697(78)90792-3. [DOI] [PubMed] [Google Scholar]
  13. Lazdunski A., Murgier M., Lazdunski C. Evidence for an aminoendopeptidase localized near the cell surface of Escherichia coli. Regulation of synthesis by inorganic phosphate. Eur J Biochem. 1975 Dec 15;60(2):349–355. doi: 10.1111/j.1432-1033.1975.tb21009.x. [DOI] [PubMed] [Google Scholar]
  14. Matin A., Rittenberg S. C. Kinetics of deoxyribonucleic acid destruction and synthesis during growth of Bdellovibrio bacteriovorus strain 109D on pseudomonas putida and escherichia coli. J Bacteriol. 1972 Sep;111(3):664–673. doi: 10.1128/jb.111.3.664-673.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Munch-Petersen A., Mygind B. Nucleoside transport systems in Escherichia coli K12: specificity and regulation. J Cell Physiol. 1976 Dec;89(4):551–559. doi: 10.1002/jcp.1040890410. [DOI] [PubMed] [Google Scholar]
  16. Munch-Petersen A. On the catabolism of deoxyribonucleosides in cells and cell extracts of Escherichia coli. Eur J Biochem. 1968 Nov;6(3):432–442. doi: 10.1111/j.1432-1033.1968.tb00465.x. [DOI] [PubMed] [Google Scholar]
  17. Murgier M., Pelissier C., Lazdunski A. Aminopeptidase N from Escherichia coli. Unusual interactions with the cell surface. Eur J Biochem. 1977 Apr 15;74(3):425–433. doi: 10.1111/j.1432-1033.1977.tb11408.x. [DOI] [PubMed] [Google Scholar]
  18. Nelson D. R., Rittenberg S. C. Incorporation of substrate cell lipid A components into the lipopolysaccharide of intraperiplasmically grown Bdellovibrio bacteriovorus. J Bacteriol. 1981 Sep;147(3):860–868. doi: 10.1128/jb.147.3.860-868.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Nelson D. R., Rittenberg S. C. Partial characterization of lipid A of intraperiplasmically grown Bdellovibrio bacteriovorus. J Bacteriol. 1981 Sep;147(3):869–874. doi: 10.1128/jb.147.3.869-874.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Neu H. C., Chou J. Release of surface enzymes in Enterobacteriaceae by osmotic shock. J Bacteriol. 1967 Dec;94(6):1934–1945. doi: 10.1128/jb.94.6.1934-1945.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nossal N. G., Heppel L. A. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J Biol Chem. 1966 Jul 10;241(13):3055–3062. [PubMed] [Google Scholar]
  22. Oakley B. R., Kirsch D. R., Morris N. R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem. 1980 Jul 1;105(2):361–363. doi: 10.1016/0003-2697(80)90470-4. [DOI] [PubMed] [Google Scholar]
  23. Rader R. L., Hochstadt J. Regulation of purine utilization in bacteria. VII. Involvement of membrane-associated nucleoside phosphorylase in the uptake and the base-mediated loss of the ribose moiety of nucleosides by Salmonella typhimurium membrane vesicles. J Bacteriol. 1976 Oct;128(1):290–301. doi: 10.1128/jb.128.1.290-301.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Rittenberg S. C., Hespell R. B. Energy efficiency of intraperiplasmic growth of Bdellovibrio bacteriovorus. J Bacteriol. 1975 Mar;121(3):1158–1165. doi: 10.1128/jb.121.3.1158-1165.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Rittenberg S. C., Langley D. Utilization of nucleoside monophosphates per Se for intraperiplasmic growth of Bdellovibrio bacteriovorus. J Bacteriol. 1975 Mar;121(3):1137–1144. doi: 10.1128/jb.121.3.1137-1144.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Switzer R. C., 3rd, Merril C. R., Shifrin S. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem. 1979 Sep 15;98(1):231–237. doi: 10.1016/0003-2697(79)90732-2. [DOI] [PubMed] [Google Scholar]
  27. Thomashow M. F., Rittenberg S. C. Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: N-deacetylation of Escherichia coli peptidoglycan amino sugars. J Bacteriol. 1978 Sep;135(3):1008–1014. doi: 10.1128/jb.135.3.1008-1014.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Thomashow M. F., Rittenberg S. C. Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: attachment of long-chain fatty acids to escherichia coli peptidoglycan. J Bacteriol. 1978 Sep;135(3):1015–1023. doi: 10.1128/jb.135.3.1015-1023.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Thomashow M. F., Rittenberg S. C. Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: solubilization of Escherichia coli peptidoglycan. J Bacteriol. 1978 Sep;135(3):998–1007. doi: 10.1128/jb.135.3.998-1007.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Thomashow M. F., Rittenberg S. C. Penicillin-induced formation of osmotically stable spheroplasts in nongrowing Bdellovibrio bacteriovorus. J Bacteriol. 1978 Mar;133(3):1484–1491. doi: 10.1128/jb.133.3.1484-1491.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]

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