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. 1972 Feb;126(3):503–513. doi: 10.1042/bj1260503

Regulation of dipicolinic acid biosynthesis in sporulating Bacillus cereus. Characterization of enzymic changes and analysis of mutants

M Forman 1, A Aronson 1
PMCID: PMC1178406  PMID: 4627586

Abstract

Some of the early enzymes in the lysine-biosynthetic pathway also function for dipicolinic acid synthesis in sporulating Bacillus cereus T. 1. The first enzyme, aspartokinase, loses its sensitivity to feedback inhibition by lysing. This change occurs before the time of dipicolinic acid synthesis but at a time when diaminopimelic acid is required for spore cortex formation. 2. A possible regulatory change at a branch point in the pathway was studied by examining the properties of a key enzyme, dihydrodipicolinic acid reductase. No alteration in the feedback sensitivity or sedimentation rate of this enzyme could be detected during sporulation. 3. Two mutants producing heat-sensitive spores were analysed. Both produced spores that contained decreased amounts of dipicolinic acid. Although neither was a lysine auxotroph, they both had greatly decreased activities of certain lysine-biosynthetic enzymes in sporulating cells. 4. Starvation of cells for calcium also results in the production of spores that are heat-sensitive and contain less dipicolinic acid than the control. A decreased content of one of the lysine-biosynthetic enzymes, dihydrodipicolinic acid synthetase, in calcium-starved cells could account for the lower concentration of dipicolinic acid in the spores.

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Selected References

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

  1. Aronson A. I., Henderson E., Tincher A. Participation of the lysine pathway in dipicolinic acid synthesis in Bacillus cereus T. Biochem Biophys Res Commun. 1967 Feb 21;26(4):454–460. doi: 10.1016/0006-291x(67)90568-2. [DOI] [PubMed] [Google Scholar]
  2. BLACK S. H., HASHIMOTO T., GERHARDT P. Calcium reversal of the heat susceptibility and dipicolinate deficiency of spores formed "endotrophically" in water. Can J Microbiol. 1960 Apr;6:213–224. doi: 10.1139/m60-023. [DOI] [PubMed] [Google Scholar]
  3. BLACK S., WRIGHT N. G. Aspartic beta-semialdehyde dehydrogenase and aspartic beta-semialdehyde. J Biol Chem. 1955 Mar;213(1):39–50. [PubMed] [Google Scholar]
  4. Bach M. L., Gilvarg C. Biosynthesis of dipicolinic acid in sporulating Bacillus megaterium. J Biol Chem. 1966 Oct 10;241(19):4563–4564. [PubMed] [Google Scholar]
  5. Bukhari A. I., Taylor A. L. Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli. J Bacteriol. 1971 Mar;105(3):844–854. doi: 10.1128/jb.105.3.844-854.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dvorak H. F. Metallo-enzymes released from Escherichia coli by osmotic shock. I. Selective depression of enzymes in cells grown in the presence of ethylenediaminetetraacetate. J Biol Chem. 1968 May 25;243(10):2640–2646. [PubMed] [Google Scholar]
  7. Farkas W., Gilvarg C. The reduction step in diaminopimelic acid biosynthesis. J Biol Chem. 1965 Dec;240(12):4717–4722. [PubMed] [Google Scholar]
  8. Fish W. W., Mann K. G., Tanford C. The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride. J Biol Chem. 1969 Sep 25;244(18):4989–4994. [PubMed] [Google Scholar]
  9. Fukuda A., Gilvarg C. The relationship of dipicolinate and lysine biosynthesis in Bacillus megaterium. J Biol Chem. 1968 Jul 25;243(14):3871–3876. [PubMed] [Google Scholar]
  10. GOLLAKOTA K. G., HALVORSON H. O. Biochemical changes occurring during sporulation of Bacillus cereus. Inhibition of sporulation by alpha-picolinic acid. J Bacteriol. 1960 Jan;79:1–8. doi: 10.1128/jb.79.1.1-8.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Grandgenett D. P., Stahly D. P. Diaminopimelate decarboxylase of sporulating bacteria. J Bacteriol. 1968 Dec;96(6):2099–2109. doi: 10.1128/jb.96.6.2099-2109.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. JANSSEN F. W., LUND A. J., ANDERSON L. E. Colorimetric assay for dipicolinic acid in bacterial spores. Science. 1958 Jan 3;127(3288):26–27. doi: 10.1126/science.127.3288.26. [DOI] [PubMed] [Google Scholar]
  13. Kornberg A., Spudich J. A., Nelson D. L., Deutscher M. P. Origin of proteins in sporulation. Annu Rev Biochem. 1968;37:51–78. doi: 10.1146/annurev.bi.37.070168.000411. [DOI] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Levisohn S., Aronson A. I. Regulation of extracellular protease production in Bacillus cereus. J Bacteriol. 1967 Mar;93(3):1023–1030. doi: 10.1128/jb.93.3.1023-1030.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  17. NAKATA H. M. ORGANIC NUTRIENTS REQUIRED FOR GROWTH AND SPORULATION OF BACILLUS CEREUS. J Bacteriol. 1964 Nov;88:1522–1524. doi: 10.1128/jb.88.5.1522-1524.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. POWELL J. F. Isolation of dipicolinic acid (pyridine-2:6-dicarboxylic acid) from spores of Bacillus megatherium. Biochem J. 1953 May;54(2):210–211. doi: 10.1042/bj0540210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pitel D. W., Gilvarg C. Mucopeptide metabolism during growth and sporulation in Bacillus megaterium. J Biol Chem. 1970 Dec 25;245(24):6711–6717. [PubMed] [Google Scholar]
  20. Rosner A., Paulus H. Regulation of aspartokinase in Bacillus subtilis. The separation and properties of two isofunctional enzymes. J Biol Chem. 1971 May 10;246(9):2965–2971. [PubMed] [Google Scholar]
  21. Sadoff H. L., Celikkol E., Engelbrecht H. L. Conversion of bacterial aldolase from vegetative to spore form by a sporulation-specific protease. Proc Natl Acad Sci U S A. 1970 Jul;66(3):844–849. doi: 10.1073/pnas.66.3.844. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schlesinger M. J. The reversible dissociation of the alkaline phosphatase of Escherichia coli. II. Properties of the subunit. J Biol Chem. 1965 Nov;240(11):4293–4298. [PubMed] [Google Scholar]
  23. VINTER V. Spores of microorganisms. IX. Gradual development of the resistant structure of bacterial endospores. Folia Microbiol (Praha) 1962 Mar;7:115–120. doi: 10.1007/BF02927234. [DOI] [PubMed] [Google Scholar]
  24. Yugari Y., Gilvarg C. The condensation step in diaminopimelate synthesis. J Biol Chem. 1965 Dec;240(12):4710–4716. [PubMed] [Google Scholar]

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